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It occurs as a by-product of bacterial metabolism and involves a combination of chemical changes in the extracellular environment, e.g. pH increase, and presence of nucleation sites on the cell surface or extracellular substances produced by the bacteria. However, the molecular mechanisms underpinning MICP and the interplay between the contributing factors remain poorly understood, thus placing barriers to the full biotechnological and synthetic biology exploitation of bacterial biomineralisation. In this study, we adopted a bottom-up approach of systematically engineering Bacillus subtilis, which has no detectable intrinsic MICP activity, for biomineralisation. We showed that heterologous production of urease can induce MICP by local increases in extracellular pH, and this can be enhanced by co-expression of urease accessory genes for urea and nickel uptake, depending on environmental conditions. MICP can be strongly enhanced by biofilm-promoting conditions, which appeared to be mainly driven by production of exopolysaccharide, while the protein component of the biofilm matrix was dispensable. Attempts to modulate the cell surface charge of B. subtilis had surprisingly minor effects, and our results suggest this organism may intrinsically have a very negative cell surface, potentially predisposing it for MICP activity. Our findings give insights into the molecular mechanisms driving MICP in an application-relevant chassis organism and the genetic elements that can be used to engineer de novo or enhanced biomineralisation. This study also highlights mutual influences between the genetic drivers and the chemical composition of the surrounding environment in determining the speed, spatial distribution and resulting mineral crystals of MICP. Taken together, these data pave the way for future rational design of synthetic precipitator strains optimised for specific applications.",{"EN":185,"VI":186},"Genetic optimisation of bacteria-induced calcite precipitation in Bacillus subtilis","Tối ưu hóa di truyền quá trình kết tủa calcit do vi khuẩn cảm ứng ở Bacillus subtilis",{"VOID":188},"Anbu P, Kang C-H, Shin Y-J, So J-S. Formations of calcium carbonate minerals by bacteria and its multiple applications. SpringerPlus. 2016;5:250.\nZhu T, Dittrich M. Carbonate precipitation through microbial activities in natural environment, and their potential in biotechnology: a review. Front Bioeng Biotechnol. 2016;4:4.\nJusto-Reinoso I, Heath A, Gebhard S, Paine K. Aerobic non-ureolytic bacteria-based self-healing cementitious composites: a comprehensive review. J Build Eng. 2021;42:102834.\nDe Muynck W, De Belie N, Verstraete W. Microbial carbonate precipitation in construction materials: a review. 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Wall teichoic acids of gram-positive bacteria. Annu Rev Microbiol. 2013;67:313–36.\nRevilla-Guarinos A, Gebhard S, Mascher T, Zúñiga M. Defence against antimicrobial peptides: different strategies in Firmicutes. Environ Microbiol. 2014;16(5):1225–37.\nKingston AW, Liao X, Helmann JD. Contributions of the σW, σM, and σX regulons to the lantibiotic resistome of Bacillus subtilis. Mol Microbiol. 2013;90(3):502–518.\nMarvasi M, Visscher PT, Casillas Martinez L. Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis. FEMS Microbiol Lett. 2010;313(1):1–9.\nOmoike A, Chorover J. Spectroscopic study of extracellular polymeric substances from Bacillus subtilis: aqueous chemistry and adsorption effects. Biomacromolecules. 2004;5(4):1219–30.\nBranda SS, Chu F, Kearns DB, Losick R, Kolter R. A major protein component of the Bacillus subtilis biofilm matrix. Mol Microbiol. 2006;59(4):1229–38.\nBranda SS, González-Pastor JE, Dervyn E, Ehrlich SD, Losick R, Kolter R. Genes involved in formation of structured multicellular communities by Bacillus subtilis. J Bacteriol. 2004;186(12):3970–9.\nOppenheimer-Shaanan Y, Sibony-Nevo O, Bloom-Ackermann Z, Suissa R, Steinberg N, Kartvelishvily E, et al. Spatio-temporal assembly of functional mineral scaffolds within microbial biofilms. NPJ Biofilms Microbiomes. 2016;2(1):15031–10.\nKim JK, Mulrooney SB, Hausinger RP. Biosynthesis of active Bacillus subtilis urease in the absence of known urease accessory proteins. J Bacteriol. 2005;187(20):7150–4.\nMa W, Liu Y, Lv X, Li J, Du G, Liu L. Combinatorial pathway enzyme engineering and host engineering overcomes pyruvate overflow and enhances overproduction of N-acetylglucosamine in Bacillus subtilis. Microb Cell Fact.; 2019;18:1.\nBoquet E, Boronat A, Ramos-Cormenzana A. 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J Biol Eng. 2013;7(1):29.\nMascher T, Margulis NG, Wang T, Ye RW, Helmann JD. Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon. Mol Microbiol. 2003;50(5):1591–604.\nKearns DB, Chu F, Branda SS, Kolter R, Losick R. A master regulator for biofilm formation by Bacillus subtilis. Mol Microbiol. 2005;55(3):739–49.\nSoon RL, Nation RL, Cockram S, Moffatt JH, Harper M, Adler B, et al. Different surface charge of colistin-susceptible and -resistant Acinetobacter baumannii cells measured with zeta potential as a function of growth phase and colistin treatment. J Antimicrob Chemother. 2011;66(1):126–33.\nStaroń A, Finkeisen DE, Mascher T. Peptide antibiotic sensing and detoxification modules of Bacillus subtilis. Antimicrob Agents Chemother. 2011;55(2):515–25.\nOkyay TO, Rodrigues DF. High throughput colorimetric assay for rapid urease activity quantification. J Microbiol Methods. 2013;95(3):324–6.\nKingston AW, Zhao H, Cook GM, Helmann JD. Accumulation of heptaprenyl diphosphate sensitizes Bacillus subtilis to bacitracin: implications for the mechanism of resistance mediated by the BceAB transporter. Mol Microbiol. 2014;93(1):37–49.\nDerré I, Rapoport G, Msadek T. The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37 degrees C. Mol Microbiol. 2000;38(2):335–47.\nGuérout-Fleury AM, Shazand K, Frandsen N, Stragier P. Antibiotic-resistance cassettes for Bacillus subtilis. Gene. 1996;167(1-2):335–6.",{"VOID":190},"10.1186\u002Fs12934-021-01704-1","PUBLICATION","VERIFIED","2024-12-21T20:09:56.366+00:00","Auto Verify",[196],"VI","https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12934-021-01704-1",[199,215,231],{"id":200,"sortIndex":21,"researcher":20,"roles":201,"affiliations":203,"properties":212,"displayName":214,"givenName":20,"familyName":20},"e042ba99-484e-4d9e-8360-d1eada7309cd",[202],"AUTHOR",[204],{"id":205,"sortIndex":21,"affiliation":206,"properties":20},"7124565e-3b08-4f76-942b-ad79d0749a71",{"id":205,"createTime":20,"updateTime":20,"relativeEntities":207,"slug":20,"properties":208,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":211,"statistic":20},[],{"title":209},{"VI":210},"Department of Biology and Biochemistry, Milner Centre for Evolution, University of Bath, Claverton Down, Bath, UK",[],{"title":213},{"VI":214},"Timothy D. Hoffmann",{"id":216,"sortIndex":217,"researcher":20,"roles":218,"affiliations":219,"properties":228,"displayName":230,"givenName":20,"familyName":20},"9b10c41b-b9e5-4b80-b4d6-71f97a132d6a",1,[202],[220],{"id":221,"sortIndex":21,"affiliation":222,"properties":20},"dd50eb89-bafe-4df3-9755-c31471a30232",{"id":221,"createTime":20,"updateTime":20,"relativeEntities":223,"slug":20,"properties":224,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":227,"statistic":20},[],{"title":225},{"VI":226},"Department of Architecture and Civil Engineering, BRE Centre for Innovative Construction Materials, University of Bath, Bath, United Kingdom",[],{"title":229},{"VI":230},"Kevin Paine",{"id":232,"sortIndex":110,"researcher":20,"roles":233,"affiliations":234,"properties":241,"displayName":243,"givenName":20,"familyName":20},"f33f315a-64d7-4e63-9ede-138a79774afb",[202],[235],{"id":205,"sortIndex":21,"affiliation":236,"properties":20},{"id":205,"createTime":20,"updateTime":20,"relativeEntities":237,"slug":20,"properties":238,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":240,"statistic":20},[],{"title":239},{"VI":210},[],{"title":242},{"VI":243},"Susanne Gebhard","ARTICLE",{"url":197,"publisher":246,"properties":295},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":247,"slug":10,"properties":248,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":251,"manageAffiliations":264,"indexDatabases":275,"url":20,"thumbnailPath":20,"statistic":290,"gsStatistic":20,"type":170,"analyzePriority":20},[],{"issn":249,"title":250},{"VOID":13},{"EN":15},[252,256,260],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":253,"label":254,"description":255,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":257,"label":258,"description":259,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":261,"label":262,"description":263,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},[265,270],{"id":43,"createTime":20,"updateTime":20,"relativeEntities":266,"slug":20,"properties":267,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":269,"statistic":20},[],{"title":268},{"EN":47},[],{"id":50,"createTime":20,"updateTime":20,"relativeEntities":271,"slug":20,"properties":272,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":274,"statistic":20},[],{"title":273},{"EN":54},[],[276,283],{"id":58,"indexDatabase":277,"url":69,"indexYears":70,"academicFieldIds":282,"indexDatabaseRanking":75},{"id":60,"createTime":20,"updateTime":20,"relativeEntities":278,"label":279,"description":280,"key":66,"publicationTags":281,"standard":20},[],{"EN":63,"VI":63},{"EN":63,"VI":65},[68],[72,73,74],{"id":77,"indexDatabase":284,"url":90,"indexYears":20,"academicFieldIds":289,"indexDatabaseRanking":20},{"id":79,"createTime":20,"updateTime":20,"relativeEntities":285,"label":286,"description":287,"key":86,"publicationTags":288,"standard":20},[],{"EN":82,"VI":82},{"EN":84,"VI":85},[88,89],[92],{"impactFactor":21,"impactFactorByYear":291,"i10Index":106,"i10IndexLast5Year":107,"totalPublication":108,"totalPublicationByYear":292,"totalCitation":130,"totalCitationByYear":293,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":294,"hindexLast5Year":169,"hindex":169},{"2012":95,"2013":96,"2014":97,"2015":97,"2016":98,"2017":99,"2018":100,"2019":101,"2020":102,"2021":103,"2022":104,"2023":105},{"2002":110,"2003":111,"2004":112,"2005":113,"2006":114,"2007":115,"2008":115,"2009":116,"2010":117,"2011":118,"2012":119,"2013":120,"2014":121,"2015":122,"2016":122,"2017":123,"2018":124,"2019":125,"2020":125,"2021":126,"2022":127,"2023":128,"2024":129},{"2005":132,"2006":133,"2007":134,"2008":135,"2009":136,"2010":137,"2011":138,"2012":139,"2013":140,"2014":141,"2015":142,"2016":143,"2017":144,"2018":145,"2019":146,"2020":147,"2021":148,"2022":124},{"2005":151,"2006":152,"2007":153,"2008":154,"2009":155,"2010":156,"2011":157,"2012":158,"2013":159,"2014":160,"2015":161,"2016":162,"2017":163,"2018":164,"2019":165,"2020":166,"2021":167,"2022":168},{"pages":296,"volume":298},{"VOID":297},"1-19",{"VOID":299},"20","2021-11-18",2021,[88,75],false,{"id":305,"createTime":306,"updateTime":307,"relativeEntities":308,"slug":309,"properties":310,"entityType":191,"verifyStatus":192,"verifyTime":320,"verifyNote":194,"languages":20,"translateLanguages":321,"viewCount":21,"primaryUrl":322,"fullTextUrl":20,"authors":323,"publicationType":244,"publisherRelationship":422,"citationCount":20,"citationInfo":20,"publishDate":476,"publishYear":477,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":478,"openAccess":20,"references":20,"isForceReanalyzing":303},"41c206a7-75da-4b52-99ee-9394d406127c","2023-11-28T13:13:51.763+00:00","2026-09-10T11:17:07.577+00:00",[],"Exopolysaccharides-from-vaginal-lactobacilli-modulate-microbial-biofilms",{"abstract":311,"title":313,"references":316,"doi":318},{"EN":312},"Exopolysaccharides (EPS) secreted by beneficial lactobacilli exert a plethora of positive activities, but little is known about their effects on biofilms of opportunistic vaginal pathogens and especially on biofilms of lactobacilli themselves. Here, the EPS produced by six vaginal lactobacilli, belonging to Lactobacillus crispatus (BC1, BC4, BC5) and Lactobacillus gasseri (BC9, BC12, BC14) species were isolated from cultural supernatants and lyophilized. Lactobacillus EPS were chemically characterized in terms of monosaccharide composition by liquid chromatography (LC) analysis coupled to UV and mass spectrometry (MS) detection. Moreover, the ability of EPS (0.1, 0.5, 1 mg\u002FmL) to stimulate the biofilm formation of lactobacilli and to inhibit the formation of pathogens’ biofilms was evaluated by crystal violet (CV) staining and 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide (MTT) assay. Isolated EPS (yields 133–426 mg\u002FL) were heteropolysaccharides mainly composed of d-mannose (40–52%) and d-glucose (11–30%). For the first time we demonstrated that Lactobacillus EPS were able to stimulate in a dose-dependent manner (p \u003C 0.05) the formation of biofilms of ten strains belonging to L. crispatus, L. gasseri and Limosilactobacillus vaginalis species, in terms of cell viability (84–282% increase at 1 mg\u002FmL) and especially biofilm biomass (40–195% increase at 1 mg\u002FmL), quantified with MTT assay and CV staining, respectively. EPS released from L. crispatus and L. gasseri were found to better stimulate the biofilms of the same producer species rather than that of other species, including producing strains themselves and other strains. Conversely, the biofilm formation of bacterial (Escherichia coli, Staphylococcus spp., Enterococcus spp. and Streptococcus agalactiae) and fungal (Candida spp.) pathogens was inhibited. The anti-biofilm activity was dose-dependent and was more marked for L. gasseri-derived EPS (inhibition up to 86%, 70%, and 58% at 1 mg\u002FmL, 0.5 mg\u002FmL, and 0.1 mg\u002FmL, respectively), whilst L. crispatus-derived EPS resulted overall less efficient (inhibition up to 58% at 1 mg\u002FmL and 40% at 0.5 mg\u002FmL) (p \u003C 0.05). Lactobacilli-derived EPS favour the biofilm formation of lactobacilli preventing, at the same time, that of opportunistic pathogens. These results support the possible employment of EPS as postbiotics in medicine as a therapeutic\u002Fpreventive strategy to counteract vaginal infections.",{"EN":314,"VI":315},"Exopolysaccharides from vaginal lactobacilli modulate microbial biofilms","Exopolysaccharide từ vi khuẩn lactobacilli âm đạo điều hòa màng sinh học vi sinh vật",{"VOID":317},"Angelin J, Kavitha M. Exopolysaccharides from probiotic bacteria and their health potential. Int J Biol Macromol. 2020;162:853–65.\nNwodo UU, Green E, Okoh AI. Bacterial exopolysaccharides: functionality and prospects. Int J Mol Sci. 2012;13:14002–15.\nBhat B, Bajaj BK. Hypocholesterolemic potential and bioactivity spectrum of an exopolysaccharide from a probiotic isolate Lactobacillus paracasei M7. Bioact Carbohydr Dietary Fibre. 2019;19: 100191.\nKumar AS, Mody K, Jha B. Bacterial exopolysaccharides—A perception. J Basic Microbiol. 2007;47:103–17.\nBadel S, Bernardi T, Michaud P. New perspectives for Lactobacilli exopolysaccharides. Biotechnol Adv. 2011;29:54–66.\nSilva LA, Lopes Neto JHP, Cardarelli HR. Exopolysaccharides produced by Lactobacillus plantarum: technological properties, biological activity, and potential application in the food industry. Ann Microbiol. 2019;69:321–8.\nRavel J, Gajer P, Abdo Z, Schneider GM, Koenig SSK, McCulle SL, et al. Vaginal microbiome of reproductive-age women. Proc Natl Acad Sci. 2011;108:4680–7.\nParolin C, Frisco G, Foschi C, Giordani B, Salvo M, Vitali B, et al. Lactobacillus crispatus BC5 interferes with chlamydia trachomatis infectivity through integrin modulation in cervical cells. Front Microbiol. 2018;9:2630.\nÑahui Palomino RA, Vanpouille C, Laghi L, Parolin C, Melikov K, Backlund P, et al. Extracellular vesicles from symbiotic vaginal lactobacilli inhibit HIV-1 infection of human tissues. Nat Commun. 2019;10:5656.\nde Gregorio PR, Parolin C, Abruzzo A, Luppi B, Protti M, Mercolini L, et al. Biosurfactant from vaginal Lactobacillus crispatus BC1 as a promising agent to interfere with Candida adhesion. Microb Cell Fact. 2020;19:133.\nBiliavska L, Pankivska Y, Povnitsa O, Zagorodnya S. Antiviral activity of exopolysaccharides produced by lactic acid bacteria of the genera Pediococcus, Leuconostoc and Lactobacillus against human adenovirus type 5. Medicina. 2019;55:519.\nRani RP, Anandharaj M, David RA. Characterization of a novel exopolysaccharide produced by Lactobacillus gasseri FR4 and demonstration of its in vitro biological properties. Int J Biol Macromol. 2018;109:772–83.\nRiaz Rajoka MS, Jin M, Haobin Z, Li Q, Shao D, Jiang C, et al. Functional characterization and biotechnological potential of exopolysaccharide produced by Lactobacillus rhamnosus strains isolated from human breast milk. LWT. 2018;89:638–47.\nWang J, Wu T, Fang X, Min W, Yang Z. Characterization and immunomodulatory activity of an exopolysaccharide produced by Lactobacillus plantarum JLK0142 isolated from fermented dairy tofu. Int J Biol Macromol. 2018;115:985–93.\nGórska S, Sandstrom C, Wojas-Turek J, Rossowska J, Pajtasz-Piasecka E, Brzozowska E, et al. Structural and immunomodulatory differences among lactobacilli exopolysaccharides isolated from intestines of mice with experimentally induced inflammatory bowel disease. Sci Rep. 2016;6:37613.\nDilna SV, Surya H, Aswathy RG, Varsha KK, Sakthikumar DN, Pandey A, et al. Characterization of an exopolysaccharide with potential health-benefit properties from a probiotic Lactobacillus plantarum RJF4. LWT Food Sci Technol. 2015;64:1179–86.\nSungur T, Aslim B, Karaaslan C, Aktas B. Impact of exopolysaccharides (EPSs) of Lactobacillus gasseri strains isolated from human vagina on cervical tumor cells (HeLa). Anaerobe. 2017;47:137–44.\nKim Y, oh S, Kim SH. Released exopolysaccharide (r-EPS) produced from probiotic bacteria reduce biofilm formation of enterohemorrhagic Escherichia coli O157:H7. Biochem Biophys Res Commun. 2009;379:324–9.\nLi W, Ji J, Rui X, Yu J, Tang W, Chen X, et al. Production of exopolysaccharides by Lactobacillus helveticus MB2-1 and its functional characteristics in vitro. LWT Food Sci Technol. 2014;59:732–9.\nWang J, Zhao X, Yang Y, Zhao A, Yang Z. Characterization and bioactivities of an exopolysaccharide produced by Lactobacillus plantarum YW32. Int J Biol Macromol. 2015;74:119–26.\nSarikaya H, Sarikaya H, Sarikaya H. Assessment of anti-biofilm activity and bifidogenic growth stimulator (BGS) effect of lyophilized exopolysaccharides (l-EPSs) from Lactobacilli strains. Int J Food Prop. 2017;20:362–71.\nHall-Stoodley L, Costerton JW, Stoodley P. Bacterial biofilms: from the natural environment to infectious diseases. Nat Rev Microbiol. 2004;2:95–108.\nLi Z, Behrens AM, Ginat N, Tzeng SY, Lu X, Sivan S, et al. Biofilm-inspired encapsulation of probiotics for the treatment of complex infections. Adv Mater. 2018;30:1803925.\nIsmail B, Nampoothiri KM. Production, purification and structural characterization of an exopolysaccharide produced by a probiotic Lactobacillus plantarum MTCC 9510. Arch Microbiol. 2010;192:1049–57.\nLv Y, Yang X, Zhao Y, Ruan Y, Yang Y, Wang Z. Separation and quantification of component monosaccharides of the tea polysaccharides from Gynostemma pentaphyllum by HPLC with indirect UV detection. Food Chem. 2009;112:742–6.\nvan Geel-Schutten GH, Flesch F, ten Brink B, Smith MR, Dijkhuizen L. Screening and characterization of Lactobacillus strains producing large amounts of exopolysaccharides. Appl Microbiol Biotechnol. 1998;50:697–703.\nDonnarumma G, Molinaro A, Cimini D, de Castro C, Valli V, de Gregorio V, et al. Lactobacillus crispatus L1: high cell density cultivation and exopolysaccharide structure characterization to highlight potentially beneficial effects against vaginal pathogens. BMC Microbiol. 2014;14:137.\nLoeffler M, Hilbig J, Velasco L, Weiss J. Usaage of in-situ exopolysaccharide-forming lactic acid bacteria in food production: Meat products—a new field of application? Compr Rev Food Sci Food Saf. 2020;19:2932–54.\nLi W, Xia X, Tang W, Ji J, Rui X, Chen X, et al. Structural characterization and anticancer activity of cell-bound exopolysaccharide from Lactobacillus helveticus MB2-1. J Agric Food Chem. 2015;63:3454–63.\nXiu L, Zhang H, Hu Z, Liang Y, Guo S, Yang M, et al. Immunostimulatory activity of exopolysaccharides from probiotic lactobacillus casei WXD030 strain as a novel adjuvant in vitro and in vivo. Food Agric Immunol. 2018;29:1086–105.\nWang M, Zhou W, Yang Y, Xing J, Xu X, Lin Y. Potential prebiotic properties of exopolysaccharides produced by a novel: Lactobacillus strain, Lactobacillus pentosus YY-112. Food Funct. 2021;12:9456–65.\nDas D, Baruah R, Goyal A. A food additive with prebiotic properties of an α-d-glucan from Lactobacillus plantarum DM5. Int J Biol Macromol. 2014;69:20–6.\nBello FD, Walter J, Hertel C, Hammes WP. In vitro study of prebiotic properties of levan-type exopolysaccharides from Lactobacilli and non-digestible carbohydrates using denaturing gradient gel electrophoresis. Syst Appl Microbiol. 2001;24:232–7.\nTsuda H, Miyamoto T. Production of exopolysaccharide by lactobacillus plantarum and the prebiotic activity of the exopolysaccharide. Food Sci Technol Res. 2010;16:87–92.\nKonieczna C, Słodziński M, Schmidt MT. Exopolysaccharides produced by Lactobacillus rhamnosus KL 53A and Lactobacillus casei Fyos affect their adhesion to enterocytes. Pol J Microbiol. 2018;67:273–81.\nDonders GGG, Bellen G, Grinceviciene S, Ruban K, Vieira-Baptista P. Aerobic vaginitis: no longer a stranger. Res Microbiol. 2017;168:845–58.\nSobel JD. Vulvovaginal candidosis. Lancet. 2007;369:1961–71.\nZanini J, da Rocha J, Feltraco VR, Gonçalves CV, Almeida PE, da Silva A, Groll V. Streptococcus agalactiae colonization and screening approach in high-risk pregnant women in southern Brazil. J Infect Dev Ctries. 2020;14(332):40.\nXu X, Peng Q, Zhang Y, Tian D, Zhang P, Huang Y, et al. A novel exopolysaccharide produced by Lactobacillus coryniformis NA-3 exhibits antioxidant and biofilm-inhibiting properties in vitro. Food Nutr Res. 2020;64:3744.\nSharma V, Harjai K, Shukla G. Effect of bacteriocin and exopolysaccharides isolated from probiotic on P aeruginosa PAO1 biofilm. Folia Microbiol. 2018;63:181–90.\nAllonsius CN, van den Broek MFL, de Boeck I, Kiekens S, Oerlemans EFM, Kiekens F, et al. Interplay between Lactobacillus rhamnosus GG and Candida and the involvement of exopolysaccharides. Microb Biotechnol. 2017;10:1753–63.\nRendueles O, Kaplan JB, Ghigo J-M. Antibiofilm polysaccharides. Environ Microbiol. 2013;15:334–46.\nAbdalla AK, Ayyash MM, Olaimat AN, Osaili TM, Al-Nabulsi AA, Shah NP, et al. Exopolysaccharides as antimicrobial agents: mechanism and spectrum of activity. Front Microbiol. 2021;12: 664395.\nHamdy AA, Elattal NA, Amin MA, Ali AE, Mansour NM, Awad GEA, et al. In vivo assessment of possible probiotic properties of Bacillus subtilis and prebiotic properties of levan. Biocatal Agric Biotechnol. 2018;13:190–7.\nGarcia-Castillo V, Marcial G, Albarracín L, Tomokiyo M, Clua P, Takahashi H, et al. The exopolysaccharide of Lactobacillus fermentum UCO-979C Is partially involved in its immunomodulatory effect and its ability to improve the resistance against Helicobacter pylori infection. Microorganisms. 2020;8:479.\nCastro-Bravo N, Wells JM, Margolles A, Ruas-Madiedo P. Interactions of surface exopolysaccharides from Bifidobacterium and Lactobacillus within the intestinal environment. Front Microbiol. 2018;9:2426.\nParolin C, Marangoni A, Laghi L, Foschi C, Ñahui Palomino RA, Calonghi N, et al. Isolation of Vaginal Lactobacilli and characterization of anti-candida activity. PLoS ONE. 2015;10: e0131220.\nZheng J, Wittouck S, Salvetti E, Franz CMAP, Harris HMB, Mattarelli P, et al. A taxonomic note on the genus Lactobacillus: description of 23 novel genera, emended description of the genus Lactobacillus beijerinck 1901, and union of Lactobacillaceae and Leuconostocaceae. Int J Syst Evol Microbiol. 2020;70:2782–858.\nFoschi C, Laghi L, Parolin C, Giordani B, Compri M, Cevenini R, et al. Novel approaches for the taxonomic and metabolic characterization of lactobacilli: Integration of 16S rRNA gene sequencing with MALDI-TOF MS and 1H-NMR. PLoS ONE. 2017;12: e0172483.\nTallon R, Bressollier P, Urdaci MC. Isolation and characterization of two exopolysaccharides produced by Lactobacillus plantarum EP56. Res Microbiol. 2003;154:705–12.\nWang W, Wang Y, Chen F, Zheng F. Comparison of determination of sugar-PMP derivatives by two different stationary phases and two HPLC detectors: C18 vs amide columns and DAD vs ELSD. J Food Compos Anal. 2021;96: 103715.\nValidation of analytical procedures: text and methodology Q2(R1). ICH harmonised tripartite guideline. international conference on harmonisation of technical requirements for registration of pharmaceuticals for human use. Chicago, USA. 2005.\nHemmingsen LM, Giordani B, Pettersen AK, Vitali B, Basnet P, Škalko-Basnet N. Liposomes-in-chitosan hydrogel boosts potential of chlorhexidine in biofilm eradication in vitro. Carbohydr Polym. 2021;262: 117939.\nAbruzzo A, Giordani B, Parolin C, de Gregorio PR, Foschi C, Cerchiara T, et al. Lactobacillus crispatus BC1 biosurfactant delivered by hyalurosomes: an advanced strategy to counteract candida biofilm. Antibiotics. 2021;10:33.\nParolin C, Croatti V, Laghi L, Giordani B, Tondi MR, de Gregorio PR, et al. Lactobacillus biofilms influence anti-Candida activity. Front Microbiol. 2021;12: 750368.\nParolin C, Croatti V, Giordani B, Vitali B. Vaginal Lactobacillus impair Candida dimorphic switching and biofilm formation. Microorganisms. 2022;10:2091.",{"VOID":319},"10.1186\u002Fs12934-023-02053-x","2025-01-12T07:08:57.223+00:00",[196],"https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12934-023-02053-x",[324,339,352,365,378,394,408],{"id":325,"sortIndex":21,"researcher":20,"roles":326,"affiliations":327,"properties":336,"displayName":338,"givenName":20,"familyName":20},"f1969a2c-916c-4acf-a3b8-81d37c481607",[202],[328],{"id":329,"sortIndex":21,"affiliation":330,"properties":20},"63f7769a-263d-428a-b77b-5efeaccc0152",{"id":329,"createTime":20,"updateTime":20,"relativeEntities":331,"slug":20,"properties":332,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":335,"statistic":20},[],{"title":333},{"VI":334},"Department of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy",[],{"title":337},{"VI":338},"Barbara Giordani",{"id":340,"sortIndex":217,"researcher":20,"roles":341,"affiliations":342,"properties":349,"displayName":351,"givenName":20,"familyName":20},"3af93d59-bd87-4f8a-97ac-8b12f6ad7443",[202],[343],{"id":329,"sortIndex":21,"affiliation":344,"properties":20},{"id":329,"createTime":20,"updateTime":20,"relativeEntities":345,"slug":20,"properties":346,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":348,"statistic":20},[],{"title":347},{"VI":334},[],{"title":350},{"VI":351},"Marina 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Parolin",{"id":379,"sortIndex":380,"researcher":20,"roles":381,"affiliations":382,"properties":391,"displayName":393,"givenName":20,"familyName":20},"afbda456-e15a-4d09-a762-71f122b7a0ff",4,[202],[383],{"id":384,"sortIndex":21,"affiliation":385,"properties":20},"610565d8-bca6-4428-8c8b-85b42350b98c",{"id":384,"createTime":20,"updateTime":20,"relativeEntities":386,"slug":20,"properties":387,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":390,"statistic":20},[],{"title":388},{"VI":389},"Yeditepe University, İstanbul, Turkey",[],{"title":392},{"VI":393},"Ülfet Erdoğan",{"id":395,"sortIndex":396,"researcher":20,"roles":397,"affiliations":398,"properties":405,"displayName":407,"givenName":20,"familyName":20},"4f0ace30-e133-43e4-8bf7-b96477c6f5db",5,[202],[399],{"id":329,"sortIndex":21,"affiliation":400,"properties":20},{"id":329,"createTime":20,"updateTime":20,"relativeEntities":401,"slug":20,"properties":402,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":404,"statistic":20},[],{"title":403},{"VI":334},[],{"title":406},{"VI":407},"Manuela Bartolini",{"id":409,"sortIndex":410,"researcher":20,"roles":411,"affiliations":412,"properties":419,"displayName":421,"givenName":20,"familyName":20},"0d1a60c0-8543-4f85-84ec-7a81426c4396",6,[202],[413],{"id":329,"sortIndex":21,"affiliation":414,"properties":20},{"id":329,"createTime":20,"updateTime":20,"relativeEntities":415,"slug":20,"properties":416,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":418,"statistic":20},[],{"title":417},{"VI":334},[],{"title":420},{"VI":421},"Beatrice Vitali",{"url":322,"publisher":423,"properties":472},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":424,"slug":10,"properties":425,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":428,"manageAffiliations":441,"indexDatabases":452,"url":20,"thumbnailPath":20,"statistic":467,"gsStatistic":20,"type":170,"analyzePriority":20},[],{"issn":426,"title":427},{"VOID":13},{"EN":15},[429,433,437],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":430,"label":431,"description":432,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":434,"label":435,"description":436,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":438,"label":439,"description":440,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},[442,447],{"id":43,"createTime":20,"updateTime":20,"relativeEntities":443,"slug":20,"properties":444,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":446,"statistic":20},[],{"title":445},{"EN":47},[],{"id":50,"createTime":20,"updateTime":20,"relativeEntities":448,"slug":20,"properties":449,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":451,"statistic":20},[],{"title":450},{"EN":54},[],[453,460],{"id":58,"indexDatabase":454,"url":69,"indexYears":70,"academicFieldIds":459,"indexDatabaseRanking":75},{"id":60,"createTime":20,"updateTime":20,"relativeEntities":455,"label":456,"description":457,"key":66,"publicationTags":458,"standard":20},[],{"EN":63,"VI":63},{"EN":63,"VI":65},[68],[72,73,74],{"id":77,"indexDatabase":461,"url":90,"indexYears":20,"academicFieldIds":466,"indexDatabaseRanking":20},{"id":79,"createTime":20,"updateTime":20,"relativeEntities":462,"label":463,"description":464,"key":86,"publicationTags":465,"standard":20},[],{"EN":82,"VI":82},{"EN":84,"VI":85},[88,89],[92],{"impactFactor":21,"impactFactorByYear":468,"i10Index":106,"i10IndexLast5Year":107,"totalPublication":108,"totalPublicationByYear":469,"totalCitation":130,"totalCitationByYear":470,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":471,"hindexLast5Year":169,"hindex":169},{"2012":95,"2013":96,"2014":97,"2015":97,"2016":98,"2017":99,"2018":100,"2019":101,"2020":102,"2021":103,"2022":104,"2023":105},{"2002":110,"2003":111,"2004":112,"2005":113,"2006":114,"2007":115,"2008":115,"2009":116,"2010":117,"2011":118,"2012":119,"2013":120,"2014":121,"2015":122,"2016":122,"2017":123,"2018":124,"2019":125,"2020":125,"2021":126,"2022":127,"2023":128,"2024":129},{"2005":132,"2006":133,"2007":134,"2008":135,"2009":136,"2010":137,"2011":138,"2012":139,"2013":140,"2014":141,"2015":142,"2016":143,"2017":144,"2018":145,"2019":146,"2020":147,"2021":148,"2022":124},{"2005":151,"2006":152,"2007":153,"2008":154,"2009":155,"2010":156,"2011":157,"2012":158,"2013":159,"2014":160,"2015":161,"2016":162,"2017":163,"2018":164,"2019":165,"2020":166,"2021":167,"2022":168},{"pages":473,"volume":474},{"VOID":297},{"VOID":475},"22","2023-03-08",2023,[88,75],{"id":480,"createTime":481,"updateTime":482,"relativeEntities":483,"slug":484,"properties":485,"entityType":191,"verifyStatus":192,"verifyTime":495,"verifyNote":194,"languages":20,"translateLanguages":496,"viewCount":21,"primaryUrl":497,"fullTextUrl":20,"authors":498,"publicationType":244,"publisherRelationship":564,"citationCount":20,"citationInfo":20,"publishDate":619,"publishYear":620,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":621,"openAccess":20,"references":20,"isForceReanalyzing":303},"105ed18e-240f-489c-828d-e96d44410198","2024-02-11T07:56:29.833+00:00","2026-09-08T06:17:57.200+00:00",[],"De-novo-resveratrol-production-through-modular-engineering-of-an-Escherichia-coli-Saccharomyces-cerevisiae-co-culture",{"abstract":486,"title":488,"references":491,"doi":493},{"EN":487},"Resveratrol is a plant secondary metabolite with diverse, potential health-promoting benefits. Due to its nutraceutical merit, bioproduction of resveratrol via microbial engineering has gained increasing attention and provides an alternative to unsustainable chemical synthesis and straight extraction from plants. However, many studies on microbial resveratrol production were implemented with the addition of water-insoluble phenylalanine or tyrosine-based precursors to the medium, limiting in the sustainable development of bioproduction. Here we present a novel coculture platform where two distinct metabolic background species were modularly engineered for the combined total and de novo biosynthesis of resveratrol. In this scenario, the upstream Escherichia coli module is capable of excreting p-coumaric acid into the surrounding culture media through constitutive overexpression of codon-optimized tyrosine ammonia lyase from Trichosporon cutaneum (TAL), feedback-inhibition-resistant 3-deoxy-d-arabinoheptulosonate-7-phosphate synthase (aroGfbr) and chorismate mutase\u002Fprephenate dehydrogenase (tyrAfbr) in a transcriptional regulator tyrR knockout strain. Next, to enhance the precursor malonyl-CoA supply, an inactivation-resistant version of acetyl-CoA carboxylase (ACC1S659A,S1157A) was introduced into the downstream Saccharomyces cerevisiae module constitutively expressing codon-optimized 4-coumarate-CoA ligase from Arabidopsis thaliana (4CL) and resveratrol synthase from Vitis vinifera (STS), and thus further improve the conversion of p-coumaric acid-to-resveratrol. Upon optimization of the initial inoculation ratio of two populations, fermentation temperature, and culture time, this co-culture system yielded 28.5 mg\u002FL resveratrol from glucose in flasks. In further optimization by increasing initial net cells density at a test tube scale, a final resveratrol titer of 36 mg\u002FL was achieved. This is first study that demonstrates the use of a synthetic E. coli–S. cerevisiae consortium for de novo resveratrol biosynthesis, which highlights its potential for production of other p-coumaric-acid or resveratrol derived biochemicals.",{"EN":489,"VI":490},"De novo resveratrol production through modular engineering of an Escherichia coli–Saccharomyces cerevisiae co-culture","Sản xuất resveratrol de novo thông qua kỹ thuật mô-đun hóa hệ đồng nuôi cấy Escherichia coli–Saccharomyces cerevisiae",{"VOID":492},"Rodriguez-Casado A. The health potential of fruits and vegetables phytochemicals: notable examples. Crit Rev Food Sci Nutr. 2016;56:1097–107.\nGambini J, Inglés M, Olaso G, Lopez-Grueso R, Bonet-Costa V, Gimeno-Mallench L, Mas-Bargues C, Abdelaziz KM, Gomez-Cabrera MC, Vina J, Borras C. Properties of resveratrol: in vitro and in vivo studies about metabolism, bioavailability, and biological effects in animal models and humans. Oxid Med Cell Longevity. 2015;2015:837042.\nRotches-Ribalta M, Andres-Lacueva C, Estruch R, Escribano E, Urpi-Sarda M. Pharmacokinetics of resveratrol metabolic profile in healthy humans after moderate consumption of red wine and grape extract tablets. Pharmacol Res. 2012;66:375–82.\nYuan S-F, Alper HS. Metabolic engineering of microbial cell factories for production of nutraceuticals. Microb Cell Fact. 2019;18:46.\nGlobal Resveratrol Market Research Report 2020. Industry Research. 2020:https:\u002F\u002Fwww.industryresearch.co\u002Fglobal-resveratrol-market-15064120.\nFarina A, Ferranti C, Marra C. An improved synthesis of resveratrol. Nat Prod Res. 2006;20:247–52.\nWang D-G, Liu W-Y, Chen G-T. A simple method for the isolation and purification of resveratrol from Polygonum cuspidatum. J Pharma Anal. 2013;3:241–7.\nTian B, Liu J. Resveratrol: a review of plant sources, synthesis, stability, modification and food application. J Sci Food Agric. 2020;100:1392–404.\nKallscheuer N, Vogt M, Stenzel A, Gätgens J, Bott M, Marienhagen J. Construction of a Corynebacterium glutamicum platform strain for the production of stilbenes and (2S)-flavanones. Metab Eng. 2016;38:47–55.\nLi M, Kildegaard KR, Chen Y, Rodriguez A, Borodina I, Nielsen J. De novo production of resveratrol from glucose or ethanol by engineered Saccharomyces cerevisiae. Metab Eng. 2015;32:1–11.\nLi M, Schneider K, Kristensen M, Borodina I, Nielsen J. Engineering yeast for high-level production of stilbenoid antioxidants. Sci Rep. 2016;6:36827.\nPalmer CM, Miller KK, Nguyen A, Alper HS. Engineering 4-coumaroyl-CoA derived polyketide production in Yarrowia lipolytica through a β-oxidation mediated strategy. Metab Eng. 2020;57:174–81.\nLim CG, Fowler ZL, Hueller T, Schaffer S, Koffas MAG. High-yield resveratrol production in engineered Escherichia coli. Appl Environ Microbiol. 2011;77:3451.\nHong J, Im D-K, Oh M-K. Investigating E. coli coculture for resveratrol production with 13C metabolic flux analysis. J Agri Food Chem. 2020;68:3466–73.\nWang J, Yang Y, Yan Y. Bioproduction of Resveratrol. In: Schwab W, Lange BM, Wüst M, editors. Biotechnology of natural products. Cham: Springer International Publishing; 2018. p. 61–79.\nBarros J, Dixon RA. Plant phenylalanine\u002Ftyrosine ammonia-lyases. Trends Plant Sci. 2020;25:66–79.\nThapa BS, Pandey PR, Park IY, Sohng KJ. Biotechnological advances in resveratrol production and its chemical diversity. Molecules. 2019;24:2571.\nPark SR, Yoon JA, Paik JH, Park JW, Jung WS, Ban Y-H, Kim EJ, Yoo YJ, Han AR, Yoon YJ. Engineering of plant-specific phenylpropanoids biosynthesis in Streptomyces venezuelae. J Biotechnol. 2009;141:181–8.\nSydor T, Schaffer S, Boles E. Considerable increase in resveratrol production by recombinant industrial yeast strains with use of rich medium. Appl Environ Microbiol. 2010;76:3361.\nSun L, Alper HS. Non-conventional hosts for the production of fuels and chemicals. Curr Opin Chem Biol. 2020;59:15–22.\nLiu X, Li X-B, Jiang J, Liu Z-N, Qiao B, Li F-F, Cheng J-S, Sun X, Yuan Y-J, Qiao J, Zhao G-R. Convergent engineering of syntrophic Escherichia coli coculture for efficient production of glycosides. Metab Eng. 2018;47:243–53.\nRoell GW, Zha J, Carr RR, Koffas MA, Fong SS, Tang YJ. Engineering microbial consortia by division of labor. Microb Cell Fact. 2019;18:35.\nMcCarty NS, Ledesma-Amaro R. Synthetic biology tools to engineer microbial communities for biotechnology. Trends Biotechnol. 2019;37:181–97.\nChen Z, Sun X, Li Y, Yan Y, Yuan Q. Metabolic engineering of Escherichia coli for microbial synthesis of monolignols. Metab Eng. 2017;39:102–9.\nZhang H, Wang X. Modular co-culture engineering, a new approach for metabolic engineering. Metab Eng. 2016;37:114–21.\nJones JA, Wang X. Use of bacterial co-cultures for the efficient production of chemicals. Curr Opin Biotechnol. 2018;53:33–8.\nCamacho-Zaragoza JM, Hernández-Chávez G, Moreno-Avitia F, Ramírez-Iñiguez R, Martínez A, Bolívar F, Gosset G. Engineering of a microbial coculture of Escherichia coli strains for the biosynthesis of resveratrol. Microb Cell Fact. 2016;15:163.\nJohnston TG, Yuan S-F, Wagner JM, Yi X, Saha A, Smith P, Nelson A, Alper HS. Compartmentalized microbes and co-cultures in hydrogels for on-demand bioproduction and preservation. Nat Commun. 2020;11:563.\nSantos CNS, Koffas M, Stephanopoulos G. Optimization of a heterologous pathway for the production of flavonoids from glucose. Metab Eng. 2011;13:392–400.\nZhou S, Lyu Y, Li H, Koffas MAG, Zhou J. Fine-tuning the (2S)-naringenin synthetic pathway using an iterative high-throughput balancing strategy. Biotechnol Bioeng. 2019;116:1392–404.\nZhang W, Liu H, Li X, Liu D, Dong X-T, Li F-F, Wang E-X, Li B-Z, Yuan Y-J. Production of naringenin from D-xylose with co-culture of E. coli and S. cerevisia. Eng Life Sci. 2017;17:1021–9.\nYuan S-F, Hsu T-C, Wang C-A, Jang M-F, Kuo Y-C, Alper HS, Guo G-L, Hwang W-S. Production of optically pure l(+)-lactic acid from waste plywood chips using an isolated thermotolerant Enterococcus faecalis SI at a pilot scale. J Ind Microbiol Biotechnol. 2018;45:961–70.\nCamus C, Ballerino P, Delgado R, Olivera-Nappa Á, Leyton C, Buschmann AH. Scaling up bioethanol production from the farmed brown macroalga Macrocystis pyrifera in Chile. Biofuels, Bioprod Biorefin. 2016;10:673–85.\nKlöckner W, Büchs J. Advances in shaking technologies. Trends Biotechnol. 2012;30:307–14.\nSuresh S, Srivastava VC, Mishra IM. Critical analysis of engineering aspects of shaken flask bioreactors. Crit Rev Biotechnol. 2009;29:255–78.\nVestergaard M, Ingmer H. Antibacterial and antifungal properties of resveratrol. Int J Antimicrob Agents. 2019;53:716–23.\nHwang D, Lim Y-H. Resveratrol antibacterial activity against Escherichia coli is mediated by Z-ring formation inhibition via suppression of FtsZ expression. Sci Rep. 2015;5:10029.\nWestman JO, Franzén CJ. Current progress in high cell density yeast bioprocesses for bioethanol production. Biotechnol J. 2015;10:1185–95.\nYuan S-F, Guo G-L, Hwang W-S. Ethanol production from dilute-acid steam exploded lignocellulosic feedstocks using an isolated multistress-tolerant Pichia kudriavzevii strain. Microb Biotechnol. 2017;10:1581–90.\nCurcio MJ, Lutz S, Lesage P. The Ty1 LTR-retrotransposon of budding yeast, Saccharomyces cerevisiae. Microbiol Spectrum. 2015;3:1–35.\nZhou K, Qiao K, Edgar S, Stephanopoulos G. Distributing a metabolic pathway among a microbial consortium enhances production of natural products. Nat Biotechnol. 2015;33:377–83.\nDai Z, Huang M, Chen Y, Siewers V, Nielsen J. Global rewiring of cellular metabolism renders Saccharomyces cerevisiae Crabtree negative. Nat Commun. 2018;9:3059.\nFrancioso A, Mastromarino P, Restignoli R, Boffi A, d’Erme M, Mosca L. Improved Stability of trans-Resveratrol in Aqueous Solutions by Carboxymethylated (1,3\u002F1,6)-β-d-Glucan. J Agri Food Chem. 2014;62:1520–5.\nThuan NH, Trung NT, Cuong NX, Van Cuong D, Van Quyen D, Malla S. Escherichia coli modular coculture system for resveratrol glucosides production. World J Microbiol Biotechnol. 2018;34:75.\nGibson DG, Young L, Chuang R-Y, Venter JC, Hutchison Iii CA, Smith HO. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods. 2009;6:343.",{"VOID":494},"10.1186\u002Fs12934-020-01401-5","2024-10-20T08:01:10.609+00:00",[196],"https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12934-020-01401-5",[499,514,527,542],{"id":500,"sortIndex":21,"researcher":20,"roles":501,"affiliations":502,"properties":511,"displayName":513,"givenName":20,"familyName":20},"8b0c7313-b5ef-4fc4-963c-facc2cc286aa",[202],[503],{"id":504,"sortIndex":21,"affiliation":505,"properties":20},"775f4d7b-ee11-4398-867f-5ec79b5085c3",{"id":504,"createTime":20,"updateTime":20,"relativeEntities":506,"slug":20,"properties":507,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":510,"statistic":20},[],{"title":508},{"VI":509},"Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, USA",[],{"title":512},{"VI":513},"Shuo-Fu Yuan",{"id":515,"sortIndex":217,"researcher":20,"roles":516,"affiliations":517,"properties":524,"displayName":526,"givenName":20,"familyName":20},"05aa4b69-f499-4697-89bd-f467309607d9",[202],[518],{"id":504,"sortIndex":21,"affiliation":519,"properties":20},{"id":504,"createTime":20,"updateTime":20,"relativeEntities":520,"slug":20,"properties":521,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":523,"statistic":20},[],{"title":522},{"VI":509},[],{"title":525},{"VI":526},"Xiunan Yi",{"id":528,"sortIndex":110,"researcher":20,"roles":529,"affiliations":530,"properties":539,"displayName":541,"givenName":20,"familyName":20},"7471b783-e27e-4b9b-abbd-aae887109bcd",[202],[531],{"id":532,"sortIndex":21,"affiliation":533,"properties":20},"981f0e41-a655-422f-b619-15db5a3a7ee8",{"id":532,"createTime":20,"updateTime":20,"relativeEntities":534,"slug":20,"properties":535,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":538,"statistic":20},[],{"title":536},{"VI":537},"Department of Chemistry, University of Washington, Seattle, USA",[],{"title":540},{"VI":541},"Trevor G. Johnston",{"id":543,"sortIndex":111,"researcher":20,"roles":544,"affiliations":545,"properties":561,"displayName":563,"givenName":20,"familyName":20},"255a972c-5a00-4f54-bd4d-e5ba6bb8dade",[202],[546,552],{"id":504,"sortIndex":21,"affiliation":547,"properties":20},{"id":504,"createTime":20,"updateTime":20,"relativeEntities":548,"slug":20,"properties":549,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":551,"statistic":20},[],{"title":550},{"VI":509},[],{"id":553,"sortIndex":217,"affiliation":554,"properties":560},"afbac1c2-73d1-4082-89d4-16ab81683afc",{"id":553,"createTime":20,"updateTime":20,"relativeEntities":555,"slug":20,"properties":556,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":559,"statistic":20},[],{"title":557},{"EN":558},"McKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, USA",[],{},{"title":562},{"VI":563},"Hal S. 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It has been used in a number of different industrial applications including food, feed, pharmaceutical, pulp\u002Fpaper industries, and second generation biofuel. To optimize the expression system of mannanase Man23 gene, two kinds of vectors and host bacteria were determined and compared. Recombinants pHY-p43-man23 and pBPS-man23 were constructed and transferred into Bacillus subtilis WB600 and Brevibacillus brevis respectively. For mannanase Man23 gene, recombinant pHY-p43-man23 expressed in Brevibacillus brevis had higher production and activity. Compared to the wild-type Bacillus subtilis B23, the production of recombinant pHY-p43-man23 in B. brevis increased by 10 times and activity increased by 21.3%. pHY-p43-man23 in B. brevis had activity at the range of 20 ~ 70°C but its optimum temperature was 50°C and had activity from pH 4 ~ 10 but its optimum pH was around 7. This demonstrated the recombinant had improved stability as well. Mannanase is an important industrial enzyme and combination of vector pHY-p43 and host Brevibacillus brevis is a novel expression system for a mannanase decoding gene. This work aims at exploring a better expression system of mannanase Man23 decoding gene for industrial application.",{"EN":632,"VI":633},"Comparison of expression systems for the extracellular production of mannanase Man23 originated from Bacillus subtilis B23","So sánh các hệ thống biểu hiện để sản xuất ngoại bào mannanase Man23 có nguồn gốc từ Bacillus subtilis B23",{"VOID":635},"Hilge M, Gloor SM, Rypniewski W, Sauer O, Heightman TD, Zimmermann W, Winterhalter K, Piontek K: High-resolution native and complex structures of thermostable beta-mannanase from thermomonospora fusca-substrate specificity in glycosyl hydrolase family 5. Structure. 1998, 6 (11): 1433-1444. 10.1016\u002FS0969-2126(98)00142-7\nSongsiriritthigul C, Buranabanyat B, Haltrich D, Yamabhai M: Efficient recombinant expression and secretion of a thermostable GH26 mannan endo-1, 4-beta-mannosidase from Bacillus licheniformis in Escherichia coli. Microb Cell Fact. 2010, 11 (9): 20-33.\nYoshida S, Sako Y, Uchida A: Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for an enzyme from Bacillus circulans K-1 that degrades guar gum. Biosci Biotechnol Biochem. 1998, 62 (3): 514-520. 10.1271\u002Fbbb.62.514\nTamaru Y, Araki T, Morishita T, Kimura T, Sakka K, Ohmiya K: Cloning, DNA sequencing, and expression of the beta-1, 4-mannanase gene from a marine bacterium, Vibrio sp. strain MA-138. J Ferment Bioeng. 1997, 83: 201-205. 10.1016\u002FS0922-338X(97)83584-2.\nFilichkin SA, Leonard JM, Monteros A, Liu P-P, Nonogaki H: A novel endo-β-mannanase gene in tomato LeMAN5 is associated with anther and pollen development. Plant Physiol. 2004, 134: 1080-1087. 10.1104\u002Fpp.103.035998\nBourgault R, Bewley JD: Variation in its C-terminal amino acids determines whether endo-beta-mannanase is active or inactive in ripening tomato fruits of different cultivars. Plant Physiol. 2002, 130 (3): 1254-1262. 10.1104\u002Fpp.011890\nLarsson AM, Anderson L, Xu B: Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus Edulis. J Mol Biol. 2006, 357 (5): 1500-1510. 10.1016\u002Fj.jmb.2006.01.044\nStålbrand H, Saloheimo A, Vehmaanpera J, Henrissat B, Penttila M: Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei beta-mannanase gene containing a cellulose binding domain. Appl Environ Microbiol. 1995, 61: 1090-1097.\nNazina TN, Tourova TP, Poltaraus AB, Novikova EV, Grigoryan AA, Ivanova AE, Lysenko AM, Petrunyaka VV, Osipov GA, Belyaev SS, Ivanov MV: Taxonomic study of aerobic thermophilic bacilli: descriptions of geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. Nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. th. Int J Syst Evol Microbiol. 2001, 51: 433-466.\nSimonen M, Palva I: Protein secretion in Bacillus species. Microbiol Rev. 1993, 57: 109-137.\nHarwood CR: Bacillus subtilis and its relatives: molecular biological and industrial workhorses. Trends Biotechnol. 1992, 10: 247-256.\nKlessen C, Malke H: Expression of the streptokinase gene from Streptococcus equisimilis in Bacillus subtilis. J Basic Microbiol. 1986, 26: 75-81. 10.1002\u002Fjobm.3620260203\nWu XC, Lee W, Tran L, Wong SL: Engineering a Bacillus subtilisexpression-secretion system with a strain deficient in six extracellular proteases. J Bacteriol. 1991, 173: 4952-4958.\nUdaka S, Yamagata H: High level secretion of heterologous proteins by Bacillus brevis. Methods Enzymol. 1993, 217: 23-33.\nKajino T, Saito Y, Asami O, Yamada Y, Hirai M, Udata S: Extracellular production of an intact and biologically active human growth hormone by Bacillus brevis. J Ind Microbiol Biotechnol. 1997, 19: 227-231. 10.1038\u002Fsj.jim.2900445\nZhang X, Tian Z, Wu Y, Zhou S, Kang D: The cloning and expression of β-mannanase gene in E. coli. Journal of Hunan Agricultural University (Natural Sciences). 2005, 31 (6): 605-608.\nHenrissat B, Davies G: Structural and sequence-based classification of glycoside hydrolases. Curr Opin Struct Biol. 1997, 7 (5): 637-644. 10.1016\u002FS0959-440X(97)80072-3\nKatrolia P, Yan Q, Zhang P, Zhou P, Yang S, Jiang Z: Gene cloning and enzymatic characterization of an alkali-tolerant endo-1, 4-β-mannanase from Rhizomucor miehei. J Agric Food Chem. 2013, 61 (2): 394-401. 10.1021\u002Fjf303319h\nVu TT, Quyen DT, Dao TT, Nquyen ST: Cloning, high-level expression, purification, and properties of a novel endo-beta-1, 4-mannanase from Bacillus subtilis G1 in Pichia pastoris. J Microbiol Biotechnol. 2012, 22 (3): 331-338. 10.4014\u002Fjmb.1106.06052\nPolitz O, Krah M, Thomsen KK, Borriss R: A highly thermostable endo-(1, 4)-beta-mannanase from the marine bacterium Rhodothermus marinus. Appl Microbiol Biotechnol. 2000, 53 (6): 715-721. 10.1007\u002Fs002530000351\nEthier N, Talbot G, Sygusch J: Gene cloning, DNA sequencing, and expression of thermostable beta-mannanase from Bacillus stearothermophilus. Appl Environ Microbiol. 1998, 64 (11): 4428-4432.\nLi Y, Yang P, Meng K, Wang Y, Luo H, Wu N, Fan Y, Yao B: Gene cloning, expression, and characterization of a novel beta-mannanase from Bacillus circulans CGMCC 1416. J Microbiol Biotechnol. 2008, 18 (1): 160-166.\nHuang JL, Bao LX, Zou HY, Che SG, Wang GX: High-level production of a cold-active B-mannanase from Bacillus subtilis BS5 and its molecular cloning and expression. Mol Gen Mikrobiol Virusol. 2012, 4: 14-17.\nHatada Y, Takeda N, Hirasawa K, Ohta Y, Usami R, Yoshida Y, Grant WD, Ito S, Horikoshi K: Sequence of the gene for a high-alkaline mannanase from an alkaliphilic Bacillus sp. strain JAMB-750, its expression in Bacillus subtilis and characterization of the recombinant enzyme. Extremophiles. 2005, 9 (6): 497-500. 10.1007\u002Fs00792-005-0460-5\nYoon KH, Lim BL: Cloning and strong expression of a Bacillus subtilis WL-3 mannanase gene in B. subtilis. J Microbiol Biotechnol. 2007, 17 (10): 1688-1694.\nChen X, Cao Y, Ding Y, Lu W, Li D: Cloning, functional expression and characterization of Aspergillus sulphureus beta-mannanase in Pichia pastoris. J Biotechnol. 2007, 128 (3): 452-461. 10.1016\u002Fj.jbiotec.2006.11.003\nLuo H, Wang Y, Wang H, Yang J, Yang Y, Huang H, Yang P, Bai Y, Shi P, Fan Y, Yao B: A novel highly acidic beta-mannanase from the acidophilic fungus Bispora sp. MEY-1: gene cloning and overexpression in Pichia pastoris. Appl Microbiol Biotechnol. 2009, 82 (3): 453-461. 10.1007\u002Fs00253-008-1766-x\nLuo H, Wang K, Huang H, Shi P, Yang P, Yao B: Gene cloning, expression, and biochemical characterization of an alkali-tolerant β-mannanase from Humicola insolens Y1. J Ind Microbiol Biotechnol. 2012, 39 (4): 547-555. 10.1007\u002Fs10295-011-1067-8\nWang Y, Shi P, Luo H, Bai Y, Huang H, Yang P, Xiong H, Yao B: Cloning, over-expression and characterization of an alkali-tolerant endo-β-1, 4-mannanase from Penicillium freii F63. J Biosci Bioeng. 2012, 113 (6): 710-714. 10.1016\u002Fj.jbiosc.2012.02.005\nLv J, Chen Y, Pei H, Yang W, Li Z, Dong B, Cao Y: Cloning, expression, and characterization of β-mannanase from Bacillus subtilis MAFIC-S11 in Pichia pastoris. Appl Biochem Biotechnol. 2013, 169 (8): 2326-2340. 10.1007\u002Fs12010-013-0156-8\nChristgau S, Kauppinen S, Vind J, Kofod LV, Dalbøge H: Expression cloning, purification and characterization of a beta-1, 4-mannanase from Aspergillus aculeatus. Biochem Mol Biol Int. 1994, 33 (5): 917-925.\nPan X, Zhou J, Tian A, Le K, Yuan H, Xue Y, Ma Y, Lu H: High level expression of a truncated β-mannanase from alkaliphilic Bacillus sp. N16-5 in Kluyveromyces cicerisporus. Biotechnol Lett. 2011, 33 (3): 565-570. 10.1007\u002Fs10529-010-0457-8\nDoi RH, Wong SL, Kawamura F: Potential use of Bacillus subtilis for secretion and production of foreign proteins. Trends Biotechnol. 1986, 9 (4): 232-235.\nChang S: Engineering for protein secretion in gram-positive bacteria. Methods Enzymol. 1987, 153: 507-516.\nPeng QZ, Zhang WC, Zhu HC: The construction of shuttle vectors of Brevibacillus brevis-Escherichia coli. Sheng Wu Gong Cheng Xue Bao. 2002, 18 (4): 438-441.\nDong X: Systematic determination manual of common bacteria. 2001, Beijing: Science Press\nSambrook J, Russell DW: Molecular cloning: a laboratory manual. 2001, New York: Cold Spring Harbor Laboratory Press\nAusubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K: Short protocols in molecular biology. 2002, USA: John Wiley & Sons Inc\nHashimoto-Gotoh T, Tsujimura A, Kuriyama K, Matsuda S: Construction and characterization of new host-vector systems for the enforcement-cloning method. Gene. 1993, 137 (2): 211-216. 10.1016\u002F0378-1119(93)90008-Q\nMcKenzie T, Hoshino T, Tanaka T, Sueoka N: The nucleotide sequence of pUB110: some salient features in relation to replication and its regulation. Plasmid. 1986, 15: 93-103. 10.1016\u002F0147-619X(86)90046-6\nTakagi H, Kadowaki K, Udaka S: Screening and characterization of protein-hyper producing bacteria without detectable exoprotease activity. Agric Biol Chem. 1989, 53: 691-699. 10.1271\u002Fbbb1961.53.691.\nMarshak DR, Kadonaga JT, Burgess RR, Knuth MW, Brennan WA, Lin S: Strategies for protein purification and characterization: a laboratory course manual. 1996, New York: Cold Spring Harbor Laboratory Press\nHogg D, Woo EJ, Bolam DN, Mckie VA, Gilbert HJ, Pickersqill RW: Crystal structure of mannanase 26a from Pseudomonas Cellulosa and analysis of residues involved in substrate binding. J Biol Chem. 2001, 276 (33): 31186-31192. 10.1074\u002Fjbc.M010290200\nSabathe F, Belaich A, Soucaille P: Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum. FEMS Microbiol Lett. 2002, 217 (1): 15-22. 10.1111\u002Fj.1574-6968.2002.tb11450.x\nGuo Y: A laboratory manual of protein electrophoresis. 1999, Beijing: Science Press",{"VOID":637},"10.1186\u002F1475-2859-12-78","2025-02-20T13:36:52.598+00:00",[196],"https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002F1475-2859-12-78",[642,657,670,683,696],{"id":643,"sortIndex":21,"researcher":20,"roles":644,"affiliations":645,"properties":654,"displayName":656,"givenName":20,"familyName":20},"b316d8f6-9e68-4a97-b52e-54b0ed8b13dd",[202],[646],{"id":647,"sortIndex":21,"affiliation":648,"properties":20},"ea414f3b-1079-4059-99c3-c0ed7f4bb54f",{"id":647,"createTime":20,"updateTime":20,"relativeEntities":649,"slug":20,"properties":650,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":653,"statistic":20},[],{"title":651},{"VI":652},"College of Bioscience and Biotechnology, Hunan Agricultural University, Changsha, China",[],{"title":655},{"VI":656},"Haiyan Zhou",{"id":658,"sortIndex":217,"researcher":20,"roles":659,"affiliations":660,"properties":667,"displayName":669,"givenName":20,"familyName":20},"bb13fc93-471e-4150-95fb-15f0ed60746b",[202],[661],{"id":647,"sortIndex":21,"affiliation":662,"properties":20},{"id":647,"createTime":20,"updateTime":20,"relativeEntities":663,"slug":20,"properties":664,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":666,"statistic":20},[],{"title":665},{"VI":652},[],{"title":668},{"VI":669},"Yong Yang",{"id":671,"sortIndex":110,"researcher":20,"roles":672,"affiliations":673,"properties":680,"displayName":682,"givenName":20,"familyName":20},"84aaaae5-966a-4bbf-878a-c3727163a8da",[202],[674],{"id":647,"sortIndex":21,"affiliation":675,"properties":20},{"id":647,"createTime":20,"updateTime":20,"relativeEntities":676,"slug":20,"properties":677,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":679,"statistic":20},[],{"title":678},{"VI":652},[],{"title":681},{"VI":682},"Xu Nie",{"id":684,"sortIndex":111,"researcher":20,"roles":685,"affiliations":686,"properties":693,"displayName":695,"givenName":20,"familyName":20},"cc9c0265-37d5-4c1e-b411-258753583d4e",[202],[687],{"id":647,"sortIndex":21,"affiliation":688,"properties":20},{"id":647,"createTime":20,"updateTime":20,"relativeEntities":689,"slug":20,"properties":690,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":692,"statistic":20},[],{"title":691},{"VI":652},[],{"title":694},{"VI":695},"Wenjiao Yang",{"id":697,"sortIndex":380,"researcher":20,"roles":698,"affiliations":699,"properties":706,"displayName":708,"givenName":20,"familyName":20},"3a569811-676a-4934-81eb-f2387018b733",[202],[700],{"id":647,"sortIndex":21,"affiliation":701,"properties":20},{"id":647,"createTime":20,"updateTime":20,"relativeEntities":702,"slug":20,"properties":703,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":705,"statistic":20},[],{"title":704},{"VI":652},[],{"title":707},{"VI":708},"Yongyao Wu",{"url":640,"publisher":710,"properties":759},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":711,"slug":10,"properties":712,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":715,"manageAffiliations":728,"indexDatabases":739,"url":20,"thumbnailPath":20,"statistic":754,"gsStatistic":20,"type":170,"analyzePriority":20},[],{"issn":713,"title":714},{"VOID":13},{"EN":15},[716,720,724],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":717,"label":718,"description":719,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":721,"label":722,"description":723,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":725,"label":726,"description":727,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},[729,734],{"id":43,"createTime":20,"updateTime":20,"relativeEntities":730,"slug":20,"properties":731,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":733,"statistic":20},[],{"title":732},{"EN":47},[],{"id":50,"createTime":20,"updateTime":20,"relativeEntities":735,"slug":20,"properties":736,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":738,"statistic":20},[],{"title":737},{"EN":54},[],[740,747],{"id":58,"indexDatabase":741,"url":69,"indexYears":70,"academicFieldIds":746,"indexDatabaseRanking":75},{"id":60,"createTime":20,"updateTime":20,"relativeEntities":742,"label":743,"description":744,"key":66,"publicationTags":745,"standard":20},[],{"EN":63,"VI":63},{"EN":63,"VI":65},[68],[72,73,74],{"id":77,"indexDatabase":748,"url":90,"indexYears":20,"academicFieldIds":753,"indexDatabaseRanking":20},{"id":79,"createTime":20,"updateTime":20,"relativeEntities":749,"label":750,"description":751,"key":86,"publicationTags":752,"standard":20},[],{"EN":82,"VI":82},{"EN":84,"VI":85},[88,89],[92],{"impactFactor":21,"impactFactorByYear":755,"i10Index":106,"i10IndexLast5Year":107,"totalPublication":108,"totalPublicationByYear":756,"totalCitation":130,"totalCitationByYear":757,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":758,"hindexLast5Year":169,"hindex":169},{"2012":95,"2013":96,"2014":97,"2015":97,"2016":98,"2017":99,"2018":100,"2019":101,"2020":102,"2021":103,"2022":104,"2023":105},{"2002":110,"2003":111,"2004":112,"2005":113,"2006":114,"2007":115,"2008":115,"2009":116,"2010":117,"2011":118,"2012":119,"2013":120,"2014":121,"2015":122,"2016":122,"2017":123,"2018":124,"2019":125,"2020":125,"2021":126,"2022":127,"2023":128,"2024":129},{"2005":132,"2006":133,"2007":134,"2008":135,"2009":136,"2010":137,"2011":138,"2012":139,"2013":140,"2014":141,"2015":142,"2016":143,"2017":144,"2018":145,"2019":146,"2020":147,"2021":148,"2022":124},{"2005":151,"2006":152,"2007":153,"2008":154,"2009":155,"2010":156,"2011":157,"2012":158,"2013":159,"2014":160,"2015":161,"2016":162,"2017":163,"2018":164,"2019":165,"2020":166,"2021":167,"2022":168},{"pages":760,"volume":762},{"VOID":761},"1-10",{"VOID":763},"12","2013-09-08",2013,[88,75],{"id":768,"createTime":769,"updateTime":770,"relativeEntities":771,"slug":772,"properties":773,"entityType":191,"verifyStatus":192,"verifyTime":785,"verifyNote":194,"languages":20,"translateLanguages":786,"viewCount":21,"primaryUrl":787,"fullTextUrl":20,"authors":788,"publicationType":244,"publisherRelationship":858,"citationCount":20,"citationInfo":20,"publishDate":908,"publishYear":909,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":910,"openAccess":20,"references":20,"isForceReanalyzing":303},"265fdd3d-9951-4068-8577-02f3d82dae8a","2024-04-06T19:35:00.120+00:00","2026-09-07T03:11:25.997+00:00",[],"Enhancement-of-cellulolytic-enzyme-production-from-intrageneric-protoplast-fusion-of-Aspergillus-species-and-evaluating-the-hydrolysate-scavenging-activity",{"abstract":774,"title":776,"keywords":779,"references":781,"doi":783},{"EN":775},"Lignocellulosic biomass provides a great starting point for the production of energy, chemicals, and fuels. The major component of lignocellulosic biomass is cellulose, the employment of highly effective enzymatic cocktails, which can be produced by a variety of microorganisms including species of the genus Aspergillus, is necessary for its utilization in a more productive manner. In this regard, molecular biology techniques should be utilized to promote the economics of enzyme production, whereas strategies like protoplast fusion could be employed to improve the efficacy of the hydrolytic process. The current study focuses on cellulase production in Aspergillus species using intrageneric protoplast fusion, statistical optimization of growth parameters, and determination of antioxidant activity of fermentation hydrolysate. Protoplast fusion was conducted between A. flavus X A. terreus (PFFT), A. nidulans X A. tamarii (PFNT) and A. oryzae X A. tubingensis (PFOT), and the resultant fusant PFNT revealed higher activity level compared with the other fusants. Thus, this study aimed to optimize lignocellulosic wastes-based medium for cellulase production by Aspergillus spp. fusant (PFNT) and studying the antioxidant effect of fermentation hydrolysate. The experimental strategy Plackett-Burman (PBD) was used to assess how culture conditions affected cellulase output, the best level of the three major variables namely, SCB, pH, and incubation temperature were then determined using Box-Behnken design (BBD). Consequently, by utilizing an optimized medium instead of a basal medium, cellulase activity increased from 3.11 U\u002Fml to 7.689 U\u002Fml CMCase. The following medium composition was thought to be ideal based on this optimization: sugarcane bagasse (SCB), 6.82 gm; wheat bran (WB), 4; Moisture, 80%; pH, 4; inoculum size, (3 × 106 spores\u002Fml); and incubation Temp. 31.8 °C for 4 days and the fermentation hydrolysate has 28.13% scavenging activities. The results obtained in this study demonstrated the significant activity of the selected fusant and the higher sugar yield from cellulose hydrolysis over its parental strains, suggesting the possibility of enhancing cellulase activity by protoplast fusion using an experimental strategy and the fermentation hydrolysate showed antioxidant activity.",{"EN":777,"VI":778},"Enhancement of cellulolytic enzyme production from intrageneric protoplast fusion of Aspergillus species and evaluating the hydrolysate scavenging activity","Tăng cường sản sinh enzym phân giải cellulose từ dung hợp protoplast cùng chi ở các loài Aspergillus và đánh giá hoạt tính thu dọn của dịch thủy phân",{"EN":780},"",{"VOID":782},"Kotarska K, Swierczynska A, Dziemianowicz W. Study on the decomposition of lignocellulosic biomass and subjecting it to alcoholic fermentation. Renewable Energy. 2015;75:389–94. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.renene.2014.10.018\nSun Z, Bottari G, Afanasenko A, Stuart MCA, Deuss PJ, Fridrich B, Barta K. Complete lignocellulose conversion with integrated catalyst recycling yielding valuable aromatics and fuels. Nat Catal. 2018;1:82–92. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41929-017-0007-z\nSarkar N, Ghosh SK, Bannerjee S, Aikat K. Bioethanol production from agricultural wastes: an overview. Renewable Energy. 2012;37:19–27. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.renene.2011.06.045\nMidorikawa GEO, Correa CL, Noronha EF, et al. Analysis of the Transcriptome in Aspergillus Tamarii during Enzymatic degradation of Sugarcane Bagasse. Front Bioeng Biotechnol. 2018;6:123. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffbioe.2018.00123\nAndlar M, Rezic T, Marđetko N, Kracher D, Ludwig R, Santek B. Lignocellulose degradation: an overview of fungi and fungal enzymes involved in lignocellulose degradation. Eng Life Sci. 2018;18:1–11. https:\u002F\u002Fdoi.org\u002F10.1002\u002Felsc.201800039\nYacout M, Abd El-Rassoul H, Makhlouf A, Metwally M. Application of gene transformation for microbial enzymes production. International Conference on Biotechnology and Environment. Alexandria, Egypt.2016.\nStrom NB, Bushley KE. Two genomes are better than one: history, genetics, and biotechnological applications of fungal heterokaryons. Fungal Biology Biotechnol. 2016;3(1):1–4. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs40694-016-0022-x\nEl-Gendy M, Al-Zahrani S, El-Bondkly A. Construction of potent recombinant strain through Intergeneric Protoplast Fusion in Endophytic Fungi for Anticancerous enzymes production using Rice Straw. Appl Biochem Biotechnol. 2017;183:30–50. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs12010-017-2429-0\nHassan MM. Influence of protoplast fusion between two Trichoderma spp. on extracellular enzymes production and antagonistic activity. Biotechnol Biotechnol Equip. 2014;28(6):1014–23. https:\u002F\u002Fdoi.org\u002F10.1080\u002F13102818.2014.978206\nLeite P, Belo I, Salgado JM. Enhancing antioxidants extraction from agro-industrial by-products by enzymatic treatment. Foods. 2022;11(22):3715. https:\u002F\u002Fdoi.org\u002F10.3390\u002Ffoods11223715\nKaur B, Sharma M, Soni R, Oberoi HS, Chadha BS. Proteome-based profiling of hypercellulase-producing strains developed through Interspecific Protoplast Fusion between Aspergillus nidulans and aspergillus tubingensis. Appl Biochem Biotechnol. 2013;169:393–407. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs12010-012-9985-0\nRodrigues PO, Gurgel LVA, Pasquini D, Badotti F, Neto AG, Baffi MA. Lignocellulose-degrading enzymes production by solid-state fermentation through fungal consortium among Ascomycetes and Basidiomycetes. Renewable Energy. 2020;145:2683–93. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.renene.2019.08.041\nLone MA, Wani MR, Bhat NA, Sheikh SA, Reshi MA. Evaluation of Cellulase Enzyme Secreted by Some Common and Stirring Rhizosphere Fungi of Juglans regia L. by DNS Method. Journal of Enzyme Research.2012; 3(1):18–22. ISSN: 0976–7657 & E-ISSN: 0976–7665. http:\u002F\u002Fwww.bioinfo.in\u002Fcontents.php?id=74\nGoda DA, Bassoons AR, Abdel Monem NM, Soliman NA. Abdel Fattah YR.Effective multi-functional biotechnological applications of protease\u002Fkeratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH). J Genetic Eng Biotechnol. 2020;18:23–35. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs43141-020-00037-7\nAbdel-Fattah YR, El Enshasy H, Anwar M, Omar H, Abolmagd E, Zahra RA. Application of factorial experimental designs for optimization of cyclosporin a production by Tolypocladium inflatum in submerged culture. J Microbiol Biotechnol. 2007;17:1930–6. https:\u002F\u002Fpubmed.ncbi.nlm.nih.gov\u002F18167438\u002F\nAbdel-Fattah YR, Soliman NA, Yousef SM, El-Helow ER. Application of experimental designs to optimize medium composition for production of thermostable lipase\u002Festerase by Geobacillus thermodenitrificans AZ1. JGEB. 2012;10:193–200. https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1687157X12000376\nAmara A, Salem SR. Logical and experimental design for phenol degradation using immobilized Acinetobacter Sp. Cult IIUM Eng J. 2010;11:89–104. https:\u002F\u002Fdoi.org\u002F10.31436\u002Fiiumej.v11i1.32\nHabib HM, Al Meqbali FT, Kamal H, Souka UD, Ibrahim WH. Bioactive Components, antioxidant and DNA damage inhibitory activities of honeys from arid regions. Food Chem. 2014;153:28–34. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.foodchem.2013.12.044\nLiu E, Li M, Abdella A, Wilkins MR. Development of a cost-effective medium for submerged production of fungal aryl alcohol oxidase using a genetically modified aspergillus nidulans strain. Bioresour Technol. 2020;305:123038. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.biortech.2020.123038\nHoffmeister D, Keller NP. Natural products of filamentous fungi: enzymes, genes, and their regulation. Nat Prod Rep. 2007;24(2):393–416. https:\u002F\u002Fdoi.org\u002F10.1039\u002Fb603084j\nLeghlimi H, Mihoubi I, Boukhalfa-Lezzar H, Djekrif-Dakhmouche S, Bennamoun L, Zahia M. Improvement of fungal cellulase production by Solid State Fermentation. Int J Sci. 2017;3:46–51. https:\u002F\u002Fdoi.org\u002F10.18483\u002FijSci.1457\nEl-Bondkly AM, El-Gendy AM. Cellulase production from agricultural residues by recombinant fusant strain of a fungal endophyte of the marine sponge Latrunculia corticate for production of ethanol. Antonie Van Leeuwenhoek. 2012;101:331–46. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs10482-011-9639-1\nRamírez-Lagunes H, Aguilar-Uscanga MG, Infanzón-Rodríguez. MI.Optimization of xylanase production from aspergillus tamarii SCBH2 using response surface methodology. Biomass Conv Bioref. 2021;1–11. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs13399-021-02046-z\nHamari Zs, Pfeiffer I, Kevei F, Ferenczy L. Preparation of mitochondrial DNA from fungal protoplasts. J Microbiol Methods. 1997;30:165–6. https:\u002F\u002Fdoi.org\u002F10.1016\u002FS0167-7012(97)00060-2\nPeberdy JF. Fungi without coats-protoplasts as tools for mycological research. Mycol Res. 1989;93:1–20. https:\u002F\u002Fdoi.org\u002F10.1016\u002FS0953-7562(89)80129-7\nPeberdy JF. Protoplasts fusion-a tool for genetic manipulation and breeding in industrial microorganisms. Enzyme Microbiol Technol. 1980;2:23–9. https:\u002F\u002Fdoi.org\u002F10.1016\u002F0141-0229(80)90004-6\nStasz TE, Harman GE, Weeden NF. Protoplast preparation and fusion in two biocontrol strains of Trichoderma Harzianum. Mycologia. 1988;80:141–50. https:\u002F\u002Fdoi.org\u002F10.2307\u002F3807788\nPe’er S, Chet I. Trichoderma protoplast fusion; a tool for improving biocontrol agents. Can J Microbiol. 1990;36:6–9. https:\u002F\u002Fdoi.org\u002F10.1139\u002Fm90-002\nSivan A, Harman GE. Improved rhizosphere competence in a protoplast fusion progeny of Trichoderma Harzianum. J Gen Microbiol. 1991;137:23–9. https:\u002F\u002Fdoi.org\u002F10.1099\u002F00221287-137-1-23\nMrinalini C, Lalithakumari D. Integration of enhanced biocontrol efficacy and fungicide tolerance in Trichoderma spp. by electrofusion. J Plant Dis Prot. 1998;105:34–40. https:\u002F\u002Fwww.jstor.org\u002Fstable\u002F43215211\nMrinalini C, Lalithakumari D. Protoplast fusion: a biotechnological tool for strain improvement of Trichoderma Sp. Curr Trends Life Sci. 1996;21:133–46. https:\u002F\u002Feurekamag.com\u002Fresearch\u002F033\u002F017\u002F033017145.php\nKumar A. Aspergillus nidulans: a potential resource of the production of the native and heterologous enzymes for industrial applications. Int J Microbiol. 2020. https:\u002F\u002Fdoi.org\u002F10.1155\u002F2020\u002F8894215\nZhang YHP, Himmel ME, Mielenz JR. Outlook for cellulase improvement: screening and selection strategies. Biotechnol Adv. 2006;24:452–81. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.biotechadv.2006.03.003\nBotella C, de Ory I, Webb C, Cantero D, Blandino A. Hydrolytic enzyme production by aspergillus awamori on grape pomace. Biochem Eng J. 2005;26:100–6. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.bej.2005.04.020\nOberoi HS, Rawat R, Chadha BS. Response surface optimization for enhanced production of cellulases with improved functional characteristics by newly isolated aspergillus Niger HN-2. Antonie Van Leeuwenhoek. 2014;105:119–34. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs10482-013-0060-9\nAbdel-Fattah YR, El-Enshasy HA, Soliman NA, El-Gendi H. Bioprocess development for production of alkaline protease by Bacillus pseudofirmus Mn6 through statistical experimental designs. J Microbiol Biotechnol. 2008;19:378–86. https:\u002F\u002Fdoi.org\u002F10.4014\u002Fjmb.0806.380\nShajahan S, Moorthy IG, Sivakumar N, Selvakumar G. Statistical modeling and optimization of cellulase production by Bacillus licheniformis NCIM 5556 isolated from the hot spring. Maharashtra, India. J King Saud Uni Sci. 2017;29:302–10. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jksus.2016.08.001\nAiba S, Humphrey AE, Millis NF. Kinetics. Biochemical Engineering. 2nd ed. New York: Academic; 1973. pp. 92–127. https:\u002F\u002Fdoi.org\u002F10.1002\u002Faic.690200435\nImran M, Anwar Z, Irshad M, Javid A, Hussain A, Ali S. Optimization of Cellulase Production from a Novel strain of Aspergillus Tubingensis IMMIS2 through response surface methodology. Biocatal Agric Biotechnol. 2017;12:191–8. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.bcab.2017.10.005\nTrinh LTP, Choi YS, Bae HJ. Production of phenolic compounds and biosugars from flower resources via several extraction processes. Ind Crops Prod. 2018;125:261–8. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.indcrop.2018.09.008\nGhandahari Yazdi AP, Barzegar M, Sahari MA, Ahmadi Gavlighi H. Optimization of the enzyme-assisted aqueous extraction of phenolic compounds from pistachio green hull. Food Sci Nutr. 2019; 7356–366. https:\u002F\u002Fdoi.org\u002F10.1002\u002Ffsn3.900",{"VOID":784},"10.1186\u002Fs12934-024-02343-y","2024-12-09T08:58:12.566+00:00",[196],"https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12934-024-02343-y",[789,804,819,832,845],{"id":790,"sortIndex":21,"researcher":20,"roles":791,"affiliations":792,"properties":801,"displayName":803,"givenName":20,"familyName":20},"47b332f6-edba-4df3-b30b-ee440e63797d",[202],[793],{"id":794,"sortIndex":21,"affiliation":795,"properties":20},"8668331d-6690-46f5-9f0e-cc8cf1b3ccfa",{"id":794,"createTime":20,"updateTime":20,"relativeEntities":796,"slug":20,"properties":797,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":800,"statistic":20},[],{"title":798},{"VI":799},"Bioprocess Development Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), City of Scientific Research and Technological Applications (SRTA-City), Universities and Research Institutes Zone, New Borg El-Arab City, Alexandria, Egypt",[],{"title":802},{"VI":803},"Doaa A. Goda",{"id":805,"sortIndex":217,"researcher":20,"roles":806,"affiliations":807,"properties":816,"displayName":818,"givenName":20,"familyName":20},"679938e0-2f47-4f27-8ec9-884eb9d3fe30",[202],[808],{"id":809,"sortIndex":21,"affiliation":810,"properties":20},"21860786-4a52-4bc3-9a9b-8ac8676690bc",{"id":809,"createTime":20,"updateTime":20,"relativeEntities":811,"slug":20,"properties":812,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":815,"statistic":20},[],{"title":813},{"VI":814},"Genetics Department, Faculty of Agriculture (El-Shatby), Alexandria, Egypt",[],{"title":817},{"VI":818},"Huda M. Shakam",{"id":820,"sortIndex":110,"researcher":20,"roles":821,"affiliations":822,"properties":829,"displayName":831,"givenName":20,"familyName":20},"26c1762b-ad4f-4356-b1c5-684186f3e946",[202],[823],{"id":809,"sortIndex":21,"affiliation":824,"properties":20},{"id":809,"createTime":20,"updateTime":20,"relativeEntities":825,"slug":20,"properties":826,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":828,"statistic":20},[],{"title":827},{"VI":814},[],{"title":830},{"VI":831},"Mai E. Metwally",{"id":833,"sortIndex":111,"researcher":20,"roles":834,"affiliations":835,"properties":842,"displayName":844,"givenName":20,"familyName":20},"acbdd2d5-81f2-4851-8469-06bea94faae5",[202],[836],{"id":809,"sortIndex":21,"affiliation":837,"properties":20},{"id":809,"createTime":20,"updateTime":20,"relativeEntities":838,"slug":20,"properties":839,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":841,"statistic":20},[],{"title":840},{"VI":814},[],{"title":843},{"VI":844},"Hager A. Abdelrasoul",{"id":846,"sortIndex":380,"researcher":20,"roles":847,"affiliations":848,"properties":855,"displayName":857,"givenName":20,"familyName":20},"1afd9c7b-f382-4c12-a23c-3691e70b31a3",[202],[849],{"id":809,"sortIndex":21,"affiliation":850,"properties":20},{"id":809,"createTime":20,"updateTime":20,"relativeEntities":851,"slug":20,"properties":852,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":854,"statistic":20},[],{"title":853},{"VI":814},[],{"title":856},{"VI":857},"Mohamed M. Yacout",{"url":20,"publisher":859,"properties":20},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":860,"slug":10,"properties":861,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":864,"manageAffiliations":877,"indexDatabases":888,"url":20,"thumbnailPath":20,"statistic":903,"gsStatistic":20,"type":170,"analyzePriority":20},[],{"issn":862,"title":863},{"VOID":13},{"EN":15},[865,869,873],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":866,"label":867,"description":868,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":870,"label":871,"description":872,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":874,"label":875,"description":876,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},[878,883],{"id":43,"createTime":20,"updateTime":20,"relativeEntities":879,"slug":20,"properties":880,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":882,"statistic":20},[],{"title":881},{"EN":47},[],{"id":50,"createTime":20,"updateTime":20,"relativeEntities":884,"slug":20,"properties":885,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":887,"statistic":20},[],{"title":886},{"EN":54},[],[889,896],{"id":58,"indexDatabase":890,"url":69,"indexYears":70,"academicFieldIds":895,"indexDatabaseRanking":75},{"id":60,"createTime":20,"updateTime":20,"relativeEntities":891,"label":892,"description":893,"key":66,"publicationTags":894,"standard":20},[],{"EN":63,"VI":63},{"EN":63,"VI":65},[68],[72,73,74],{"id":77,"indexDatabase":897,"url":90,"indexYears":20,"academicFieldIds":902,"indexDatabaseRanking":20},{"id":79,"createTime":20,"updateTime":20,"relativeEntities":898,"label":899,"description":900,"key":86,"publicationTags":901,"standard":20},[],{"EN":82,"VI":82},{"EN":84,"VI":85},[88,89],[92],{"impactFactor":21,"impactFactorByYear":904,"i10Index":106,"i10IndexLast5Year":107,"totalPublication":108,"totalPublicationByYear":905,"totalCitation":130,"totalCitationByYear":906,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":907,"hindexLast5Year":169,"hindex":169},{"2012":95,"2013":96,"2014":97,"2015":97,"2016":98,"2017":99,"2018":100,"2019":101,"2020":102,"2021":103,"2022":104,"2023":105},{"2002":110,"2003":111,"2004":112,"2005":113,"2006":114,"2007":115,"2008":115,"2009":116,"2010":117,"2011":118,"2012":119,"2013":120,"2014":121,"2015":122,"2016":122,"2017":123,"2018":124,"2019":125,"2020":125,"2021":126,"2022":127,"2023":128,"2024":129},{"2005":132,"2006":133,"2007":134,"2008":135,"2009":136,"2010":137,"2011":138,"2012":139,"2013":140,"2014":141,"2015":142,"2016":143,"2017":144,"2018":145,"2019":146,"2020":147,"2021":148,"2022":124},{"2005":151,"2006":152,"2007":153,"2008":154,"2009":155,"2010":156,"2011":157,"2012":158,"2013":159,"2014":160,"2015":161,"2016":162,"2017":163,"2018":164,"2019":165,"2020":166,"2021":167,"2022":168},"2024-03-02",2024,[88,75],{"id":912,"createTime":913,"updateTime":914,"relativeEntities":915,"slug":916,"properties":917,"entityType":191,"verifyStatus":192,"verifyTime":927,"verifyNote":194,"languages":20,"translateLanguages":928,"viewCount":21,"primaryUrl":929,"fullTextUrl":20,"authors":930,"publicationType":244,"publisherRelationship":1066,"citationCount":20,"citationInfo":20,"publishDate":1121,"publishYear":1122,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":1123,"openAccess":20,"references":20,"isForceReanalyzing":303},"6061e8ce-ccfc-4916-8d53-2fbee0cdc688","2023-12-12T05:49:18.182+00:00","2026-09-06T10:10:01.901+00:00",[],"Development-of-a-powerful-synthetic-hybrid-promoter-to-improve-the-cellulase-system-of-Trichoderma-reesei-for-efficient-saccharification-of-corncob-residues",{"abstract":918,"title":920,"references":923,"doi":925},{"EN":919},"The filamentous fungus Trichoderma reesei is a widely used workhorse for cellulase production in industry due to its prominent secretion capacity of extracellular cellulolytic enzymes. However, some key components are not always sufficient in this cellulase cocktail, making the conversion of cellulose-based biomass costly on the industrial scale. Development of strong and efficient promoters would enable cellulase cocktail to be optimized for bioconversion of biomass. In this study, a synthetic hybrid promoter was constructed and applied to optimize the cellulolytic system of T. reesei for efficient saccharification towards corncob residues. Firstly, a series of 5’ truncated promoters in different lengths were established based on the strong constitutive promoter Pcdna1. The strongest promoter amongst them was Pcdna1-3 (− 640 to − 1 bp upstream of the translation initiation codon ATG), exhibiting a 1.4-fold higher activity than that of the native cdna1 promoter. Meanwhile, the activation region (− 821 to − 622 bp upstream of the translation initiation codon ATG and devoid of the Cre1-binding sites) of the strong inducible promoter Pcbh1 was cloned and identified to be an amplifier in initiating gene expression. Finally, this activation region was fused to the strongest promoter Pcdna1-3, generating the novel synthetic hybrid promoter Pcc. This engineered promoter Pcc drove strong gene expression by displaying 1.6- and 1.8-fold stronger fluorescence intensity than Pcbh1 and Pcdna1 under the inducible condition using egfp as the reporter gene, respectively. Furthermore, Pcc was applied to overexpress the Aspergillus niger β-glucosidase BGLA coding gene bglA and the native endoglucanase EG2 coding gene eg2, achieving 43.5-fold BGL activity and 1.2-fold EG activity increase, respectively. Ultimately, to overcome the defects of the native cellulase system in T. reesei, the bglA and eg2 were co-overexpressed under the control of Pcc promoter. The bglA-eg2 double expression strain QPEB70 exhibited a 178% increase in total cellulase activity, whose cellulase system displayed 2.3- and 2.4-fold higher saccharification efficiency towards acid-pretreated and delignified corncob residues than the parental strain, respectively. The synthetic hybrid promoter Pcc was generated and employed to improve the cellulase system of T. reesei by expressing specific components. Therefore, construction of synthetic hybrid promoters would allow particular cellulase genes to be expressed at desired levels, which is a viable strategy to optimize the cellulolytic enzyme system for efficient biomass bioconversion.",{"EN":921,"VI":922},"Development of a powerful synthetic hybrid promoter to improve the cellulase system of Trichoderma reesei for efficient saccharification of corncob residues","Phát triển promoter lai tổng hợp mạnh để cải thiện hệ cellulase của Trichoderma reesei nhằm đường hoá hiệu quả bã lõi ngô",{"VOID":924},"Bischof RH, Ramoni J, Seiboth B. Cellulases and beyond: the first 70 years of the enzyme producer Trichoderma reesei. Microb Cell Fact. 2016;15(1):106.\nSeiboth B, Messner R, Gruber F, Kubicek CP. Disruption of the Trichoderma reesei cbh2 gene coding for cellobiohydrolase II leads to a delay in the triggering of cellulase formation by cellulose. J Gen Microbiol. 1992;138(6):1259–64.\nFang H, Xia L. High activity cellulase production by recombinant Trichoderma reesei ZU-02 with the enhanced cellobiohydrolase production. Bioresour Technol. 2013;144:693–7.\nMargolles-Clark E, Harman GE, Penttila M. Enhanced expression of endochitinase in trichoderma harzianum with the cbh1 promoter of Trichoderma reesei. Appl Environ Microbiol. 1996;62(6):2152–5.\nWood TM, McCrae SI. Purification and some properties of a (1→4)-β- d-glucan glucohydrolase associated with the cellulase from the fungus Penicillium funiculosum. Carbohydr Res. 1982;110(2):291–303.\nMiettinen-Oinonen A, Suominen P. Enhanced production of Trichoderma reesei endoglucanases and use of the new cellulase preparations in producing the stonewashed effect on denim fabric. Appl Environ Microbiol. 2002;68(8):3956–64.\nSaloheimo M, Kuja-Panula J, Ylösmäki E, Ward M, Penttilä M. Enzymatic properties and intracellular localization of the novel Trichoderma reesei beta-glucosidase BGLII (cel1A). Appl Environ Microbiol. 2002;68(9):4546–53.\nUusitalo JM, Nevalainen KM, Harkki AM, Knowles JK, Penttilä ME. Enzyme production by recombinant Trichoderma reesei strains. J Biotechnol. 1991;17(1):35–49.\nLiu G, Qu Y. Engineering of filamentous fungi for efficient conversion of lignocellulose: tools, recent advances and prospects. Biotechnol Adv. 2019;37(4):519–29.\nFitz E, Wanka F, Seiboth B. The promoter toolbox for recombinant gene expression in Trichoderma reesei. Front Bioeng Biotechnol. 2018;6:135.\nLi C, Lin F, Li Y, Wei W, Wang H, Qin L, Zhou Z, Li B, Wu F, Chen Z. A β-glucosidase hyper-production Trichoderma reesei mutant reveals a potential role of cel3D in cellulase production. Microb Cell Fact. 2016;15(1):151.\nHägglund P, Eriksson T, Collén A, Nerinckx W, Claeyssens M, Stålbrand H. A cellulose-binding module of the Trichoderma reesei beta-mannanase Man5A increases the mannan-hydrolysis of complex substrates. J Biotechnol. 2003;101(1):37–48.\nLi J, Wang J, Wang S, Xing M, Yu S, Liu G. Achieving efficient protein expression in Trichoderma reesei by using strong constitutive promoters. Microb Cell Fact. 2012;11:84.\nNakari-Setälä T, Penttilä M. Production of Trichoderma reesei cellulases on glucose-containing media. Appl Environ Microbiol. 1995;61(10):3650–5.\nUzbas F, Sezerman U, Hartl L, Kubicek CP, Seiboth B. A homologous production system for Trichoderma reesei secreted proteins in a cellulase-free background. Appl Microbiol Biotechnol. 2012;93(4):1601–8.\nIlmén M, Onnela ML, Klemsdal S, Keränen S, Penttilä M. Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei. Mol Gen Genet. 1996;253(3):303–14.\nTakashima S, Iikura H, Nakamura A, Masaki H, Uozumi T. Analysis of Cre1 binding sites in the Trichoderma reesei cbh1 upstream region. FEMS Microbiol Lett. 1996;145(3):361–6.\nSaloheimo A, Aro N, Ilmén M, Penttilä M. Isolation of the ace1 gene encoding a Cys(2)-His(2) transcription factor involved in regulation of activity of the cellulase promoter cbh1 of Trichoderma reesei. J Biol Chem. 2000;275(8):5817–25.\nAro N, Saloheimo A, Ilmén M, Penttilä M. ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei. J Biol Chem. 2001;276(26):24309–14.\nFurukawa T, Shida Y, Kitagami N, Mori K, Kato M, Kobayashi T, Okada H, Ogasawara W, Morikawa Y. Identification of specific binding sites for XYR1, a transcriptional activator of cellulolytic and xylanolytic genes in Trichoderma reesei. Fungal Genet Biol. 2009;46(8):564–74.\nZou G, Shi S, Jiang Y, van den Brink J, de Vries RP, Chen L, Zhang J, Ma L, Wang C, Zhou Z. Construction of a cellulase hyper-expression system in Trichoderma reesei by promoter and enzyme engineering. Microb Cell Fact. 2012;11:21.\nLiu T, Wang T, Li X, Liu X. 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Developing synthetic hybrid promoters to increase constitutive or diauxic shift-induced expression in Saccharomyces cerevisiae. FEMS Yeast Res. 2018;18(8):foy098.\nKiesenhofer DP, Mach RL, Mach-Aigner AR. Influence of cis element arrangement on promoter strength in Trichoderma reesei. Appl Environ Microbiol. 2017;84(1):1742–817.\nKo JK, Ximenes E, Kim Y, Ladisch MR. Adsorption of enzyme onto lignins of liquid hot water pretreated hardwoods. Biotechnol Bioeng. 2015;112(3):447–56.\nLima MA, Oliveira-Neto M, Kadowaki MA, Rosseto FR, Prates ET, Squina FM, Leme AF, Skaf MS, Polikarpov I. Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (GH3) β-glucosidase structure and function. J Biol Chem. 2013;288(46):32991–3005.\nSeiboth B, Hakola S, Mach RL, Suominen PL, Kubicek CP. Role of four major cellulases in triggering of cellulase gene expression by cellulose in Trichoderma reesei. 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Double-joint PCR: a PCR-based molecular tool for gene manipulations in filamentous fungi. Fungal Genet Biol. 2004;41(11):973–81.\nGhose TK. Measurement of cellulase activities. Pure Appl Chem. 1987;59(2):257–68.\nLiu K, Lin X, Yue J, Li X, Fang X, Zhu M, Lin J, Qu Y, Xiao L. High concentration ethanol production from corncob residues by fed-batch strategy. 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               \u003Cjats:title>Background\u003C\u002Fjats:title>\n                \u003Cjats:p>The intracellular molecule trehalose in \u003Cjats:italic>Saccharomyces cerevisiae\u003C\u002Fjats:italic> may have a major protective function under extreme environmental conditions. \u003Cjats:italic>NTH1\u003C\u002Fjats:italic> is one gene which expresses trehalase to degrade trehalose. Small heat shock protein 12 (\u003Cjats:italic>HSP12\u003C\u002Fjats:italic> expressed) plays a role in protecting membranes and enhancing freezing stress tolerance.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>An optimized \u003Cjats:italic>S. cerevisiae\u003C\u002Fjats:italic> CRISPR-Cpf1 genome-editing system was constructed. Multiplex genome editing using a single crRNA array was shown to be functional. \u003Cjats:italic>NTH1\u003C\u002Fjats:italic> or\u002Fand \u003Cjats:italic>HSP12\u003C\u002Fjats:italic> knockout in \u003Cjats:italic>S. cerevisiae\u003C\u002Fjats:italic> enhanced the freezing stress tolerance and improved the leavening ability after freezing and thawing.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusions\u003C\u002Fjats:title>\n                \u003Cjats:p>Deleting \u003Cjats:italic>NTH1\u003C\u002Fjats:italic> in the combination with deleting \u003Cjats:italic>HSP12\u003C\u002Fjats:italic> would strengthen the freezing tolerance and protect the cell viability from high rates of death in longer-term freezing. It provides valuable insights for breeding novel \u003Cjats:italic>S. cerevisiae\u003C\u002Fjats:italic> strains for the baking industry through a more precise, speedy, and economic genome-editing system.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":1136,"VI":1137},"Deletion of NTH1 and HSP12 increases the freeze–thaw resistance of baker’s yeast in bread dough","Xóa bỏ NTH1 và HSP12 làm tăng tính chịu đóng băng–tan băng của men nở trong bột nhào bánh mì",{"VOID":1139},"35879798",{"VOID":1141},"10.1186\u002Fs12934-022-01876-4","2025-02-19T14:04:33.134+00:00",[1144],"EN",[196],"https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12934-022-01876-4",[1148,1165],{"id":1149,"sortIndex":21,"researcher":20,"roles":1150,"affiliations":1151,"properties":1160,"displayName":1162,"givenName":20,"familyName":20},"d0d54ce1-b0a4-4526-99f4-dce9553412f6",[],[1152],{"id":1153,"sortIndex":21,"affiliation":1154,"properties":20},"a2f97a23-7ff1-4453-9568-dfcc5ae5fa2b",{"id":1153,"createTime":20,"updateTime":20,"relativeEntities":1155,"slug":20,"properties":1156,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1159,"statistic":20},[],{"title":1157},{"EN":1158},"Bioresource Collection and Research Center, Food Industry Research and Development Institute, Hsinchu, 300, Taiwan",[],{"title":1161,"openalex":1163},{"EN":1162},"Bo-Chou Chen",{"VOID":1164},"A5045052448",{"id":1166,"sortIndex":217,"researcher":20,"roles":1167,"affiliations":1168,"properties":1175,"displayName":1179,"givenName":20,"familyName":20},"f42f5044-845b-4572-9947-1ce8e84e7103",[],[1169],{"id":1153,"sortIndex":21,"affiliation":1170,"properties":20},{"id":1153,"createTime":20,"updateTime":20,"relativeEntities":1171,"slug":20,"properties":1172,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1174,"statistic":20},[],{"title":1173},{"EN":1158},[],{"orcid":1176,"title":1178,"openalex":1180},{"VOID":1177},"https:\u002F\u002Forcid.org\u002F0000-0003-0662-9435",{"EN":1179},"Horng–Chih Lin",{"VOID":1181},"A5040677061",{"url":20,"publisher":1183,"properties":1232},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1184,"slug":10,"properties":1185,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1188,"manageAffiliations":1201,"indexDatabases":1212,"url":20,"thumbnailPath":20,"statistic":1227,"gsStatistic":20,"type":170,"analyzePriority":20},[],{"issn":1186,"title":1187},{"VOID":13},{"EN":15},[1189,1193,1197],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":1190,"label":1191,"description":1192,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":1194,"label":1195,"description":1196,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":1198,"label":1199,"description":1200,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},[1202,1207],{"id":43,"createTime":20,"updateTime":20,"relativeEntities":1203,"slug":20,"properties":1204,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1206,"statistic":20},[],{"title":1205},{"EN":47},[],{"id":50,"createTime":20,"updateTime":20,"relativeEntities":1208,"slug":20,"properties":1209,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1211,"statistic":20},[],{"title":1210},{"EN":54},[],[1213,1220],{"id":58,"indexDatabase":1214,"url":69,"indexYears":70,"academicFieldIds":1219,"indexDatabaseRanking":75},{"id":60,"createTime":20,"updateTime":20,"relativeEntities":1215,"label":1216,"description":1217,"key":66,"publicationTags":1218,"standard":20},[],{"EN":63,"VI":63},{"EN":63,"VI":65},[68],[72,73,74],{"id":77,"indexDatabase":1221,"url":90,"indexYears":20,"academicFieldIds":1226,"indexDatabaseRanking":20},{"id":79,"createTime":20,"updateTime":20,"relativeEntities":1222,"label":1223,"description":1224,"key":86,"publicationTags":1225,"standard":20},[],{"EN":82,"VI":82},{"EN":84,"VI":85},[88,89],[92],{"impactFactor":21,"impactFactorByYear":1228,"i10Index":106,"i10IndexLast5Year":107,"totalPublication":108,"totalPublicationByYear":1229,"totalCitation":130,"totalCitationByYear":1230,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":1231,"hindexLast5Year":169,"hindex":169},{"2012":95,"2013":96,"2014":97,"2015":97,"2016":98,"2017":99,"2018":100,"2019":101,"2020":102,"2021":103,"2022":104,"2023":105},{"2002":110,"2003":111,"2004":112,"2005":113,"2006":114,"2007":115,"2008":115,"2009":116,"2010":117,"2011":118,"2012":119,"2013":120,"2014":121,"2015":122,"2016":122,"2017":123,"2018":124,"2019":125,"2020":125,"2021":126,"2022":127,"2023":128,"2024":129},{"2005":132,"2006":133,"2007":134,"2008":135,"2009":136,"2010":137,"2011":138,"2012":139,"2013":140,"2014":141,"2015":142,"2016":143,"2017":144,"2018":145,"2019":146,"2020":147,"2021":148,"2022":124},{"2005":151,"2006":152,"2007":153,"2008":154,"2009":155,"2010":156,"2011":157,"2012":158,"2013":159,"2014":160,"2015":161,"2016":162,"2017":163,"2018":164,"2019":165,"2020":166,"2021":167,"2022":168},{"issue":1233,"volume":1235},{"VOID":1234},"1",{"VOID":1120},{"total":380,"publishYear":1122,"statisticByYear":1237},{"2023":111,"2024":217},"2022-12-01",[88,75],[1241,1245,1249,1253,1257,1261,1265,1269,1273,1277,1281,1285,1289,1293,1297,1301,1304,1308,1312,1316,1320,1324,1328,1332,1336,1340,1344,1348,1352,1356,1360,1364,1368,1371,1375,1379,1383,1387,1391,1395,1399,1403,1407,1411,1415,1419],{"id":20,"text":1242,"url":20,"identifiers":1243},"Tanaka 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Genetics. 1969;61:377–89.",{"doi":1418},"10.1093\u002Fgenetics\u002F61.2.377",{"id":20,"text":1420,"url":20,"identifiers":1421},"Aboaba OO, Obakpolor EA. The leavening ability of baker’s yeast on dough prepared with composite flour (wheat\u002Fcassava). Afr J Food Sci. 2010;4:325–9.",{},{"id":1423,"createTime":1424,"updateTime":1425,"relativeEntities":1426,"slug":1427,"properties":1428,"entityType":191,"verifyStatus":192,"verifyTime":1440,"verifyNote":194,"languages":1441,"translateLanguages":1442,"viewCount":21,"primaryUrl":1443,"fullTextUrl":20,"authors":1444,"publicationType":244,"publisherRelationship":1587,"citationCount":21,"citationInfo":1637,"publishDate":20,"publishYear":20,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":1639,"openAccess":20,"references":1640,"isForceReanalyzing":303},"950bc5e0-b361-4d7d-acdd-f01358ce8c5e","2024-04-15T03:45:43.263+00:00","2026-09-05T07:11:33.362+00:00",[],"New-insights-into-the-dihydro-mureidomycin-biosynthesis-controlled-by-two-unusual-proteins-in-Streptomyces-roseosporus",{"openalex":1429,"abstract":1431,"title":1433,"pm":1436,"doi":1438},{"VOID":1430},"W4389612016",{"EN":1432},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:sec>\n                \u003Cjats:title>Background\u003C\u002Fjats:title>\n                \u003Cjats:p>Uridyl peptide compounds are renowned as a subclass of nucleoside antibiotics for their highly specific antibacterial activity against Gram-negative bacteria and the unique target of action. We previously activated the biosynthetic gene cluster of a uridyl peptide antibiotic, mureidomycin, in \u003Cjats:italic>Streptomyces roseosporus\u003C\u002Fjats:italic> NRRL 15998 by introducing an exogenous positive regulator gene \u003Cjats:italic>ssaA\u003C\u002Fjats:italic>, and the generated strain was designated as Sr-hA. This study aims to further explore mureidomycin analogs from Sr-hA as well as the collaborative roles of two wide-spread genes, \u003Cjats:italic>SSGG-02980\u003C\u002Fjats:italic> and \u003Cjats:italic>SSGG-03002\u003C\u002Fjats:italic> encoding putative nuclease\u002Fphosphatase and oxidoreductase respectively, in mureidomycin diversification.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>In order to understand how \u003Cjats:italic>SSGG-02980\u003C\u002Fjats:italic> and \u003Cjats:italic>SSGG-03002\u003C\u002Fjats:italic> contribute to mureidomycin biosynthesis, the gene disruption mutants and complementary strains were constructed. Mass spectrometry analyses revealed that two series of pairwise mureidomycin analogs were synthesized in Sr-hA with a two-dalton difference in molecular weight for each pair. By disruption of \u003Cjats:italic>SSGG-03002\u003C\u002Fjats:italic>, only mureidomycins with lower molecular weight (MRDs, \u003Cjats:bold>1\u003C\u002Fjats:bold>–\u003Cjats:bold>6\u003C\u002Fjats:bold>) could be specifically accumulated in the mutant (∆03002-hA), whereas the other series of products with molecular weight plus 2 Da (rMRDs, \u003Cjats:bold>1ʹ\u003C\u002Fjats:bold>–\u003Cjats:bold>6ʹ\u003C\u002Fjats:bold>) became dominant in \u003Cjats:italic>SSGG-02980\u003C\u002Fjats:italic> disruption mutant (∆02980-hA). Further comprehensive NMR analyses were performed to elucidate the structures, and three MRDs (\u003Cjats:bold>3\u003C\u002Fjats:bold>, \u003Cjats:bold>4\u003C\u002Fjats:bold>, \u003Cjats:bold>5\u003C\u002Fjats:bold>) with unsaturated double bond at C5-C6 of uracil group were characterized from ∆03002-hA. In contrast, the paired rMRDs analogs (\u003Cjats:bold>3ʹ\u003C\u002Fjats:bold>,\u003Cjats:bold> 4ʹ\u003C\u002Fjats:bold>,\u003Cjats:bold> 5ʹ\u003C\u002Fjats:bold>) from ∆SSGG-02980 corresponding to \u003Cjats:bold>3\u003C\u002Fjats:bold>, \u003Cjats:bold>4\u003C\u002Fjats:bold> and\u003Cjats:bold> 5\u003C\u002Fjats:bold> were shown to contain a single bond at this position. The results verified that SSGG-03002 participates in the reduction of uracil ring, whereas SSGG-02980 antagonizes the effect of SSGG-03002, which has been rarely recognized for a phosphatase.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusions\u003C\u002Fjats:title>\n                \u003Cjats:p>Overall, this study revealed the key roles of two wide-spread families of enzymes in \u003Cjats:italic>Streptomyces\u003C\u002Fjats:italic>. Of them, oxidoreductase, SSGG-03002, is involved in dihydro-mureidomycin biosynthesis of \u003Cjats:italic>S. roseosporus\u003C\u002Fjats:italic>, whereas nuclease\u002Fphosphatase, SSGG-02980, has an adverse effect on \u003Cjats:italic>SSGG-03002\u003C\u002Fjats:italic>. This kind of unusual regulation model between nuclease\u002Fphosphatase and oxidoreductase is unprecedented, providing new insights into the biosynthesis of mureidomycins in \u003Cjats:italic>Streptomyces\u003C\u002Fjats:italic>. The findings would be of significance for structural diversification of more uridyl peptide antibiotics against Gram-negative bacteria.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":1434,"VI":1435},"New insights into the dihydro-mureidomycin biosynthesis controlled by two unusual proteins in Streptomyces roseosporus","Những hiểu biết mới về quá trình tổng hợp sinh học dihydro-mureidomycin được kiểm soát bởi hai protein bất thường ở Streptomyces roseosporus",{"VOID":1437},"38087285",{"VOID":1439},"10.1186\u002Fs12934-023-02260-6","2025-02-12T23:32:03.370+00:00",[1144],[196],"https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12934-023-02260-6",[1445,1464,1481,1500,1517,1534,1551,1570],{"id":1446,"sortIndex":21,"researcher":20,"roles":1447,"affiliations":1448,"properties":1457,"displayName":1461,"givenName":20,"familyName":20},"2ccc7475-a938-4f7d-8637-8ca5e38304d8",[],[1449],{"id":1450,"sortIndex":21,"affiliation":1451,"properties":20},"0ce683e4-bb5b-4452-98ba-62f0a742cb73",{"id":1450,"createTime":20,"updateTime":20,"relativeEntities":1452,"slug":20,"properties":1453,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1456,"statistic":20},[],{"title":1454},{"VI":1455},"State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China",[],{"orcid":1458,"title":1460,"openalex":1462},{"VOID":1459},"https:\u002F\u002Forcid.org\u002F0000-0002-8282-5393",{"EN":1461},"Liu Ning",{"VOID":1463},"A5022773264",{"id":1465,"sortIndex":217,"researcher":20,"roles":1466,"affiliations":1467,"properties":1474,"displayName":1478,"givenName":20,"familyName":20},"ccfa67be-2818-4a13-a8d0-4d289e08761b",[],[1468],{"id":1450,"sortIndex":21,"affiliation":1469,"properties":20},{"id":1450,"createTime":20,"updateTime":20,"relativeEntities":1470,"slug":20,"properties":1471,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1473,"statistic":20},[],{"title":1472},{"VI":1455},[],{"orcid":1475,"title":1477,"openalex":1479},{"VOID":1476},"https:\u002F\u002Forcid.org\u002F0000-0001-7587-2194",{"EN":1478},"Yang 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G, Chater KF, Chandra G, Niu G, Tan H. Molecular regulation of antibiotic biosynthesis in Streptomyces. Microbiol Mol Biol Rev. 2013;77:112–43.",{"doi":1644},"10.1128\u002FMMBR.00054-12",{"id":20,"text":1646,"url":20,"identifiers":1647},"Li J, Wang W, Liu X, Tian Y, Tan H, Zhang J. A butenolide signaling system synergized with biosynthetic gene modules led to effective activation and enhancement of silent oviedomycin production in Streptomyces. Metab Eng. 2022;72:289–96.",{"doi":1648},"10.1016\u002Fj.ymben.2022.04.002",{"id":20,"text":1650,"url":20,"identifiers":1651},"Zhang J, Tan H. Microbial quorum sensing signaling molecules and their roles in the biosynthesis of natural products. Sci China Life Sci. 2023;66:2429–2432.",{"doi":1652},"10.1007\u002Fs11427-023-2389-7",{"id":20,"text":1654,"url":20,"identifiers":1655},"Niu G, Tan H. Nucleoside antibiotics: biosynthesis, regulation, and biotechnology. Trends Microbiol. 2015;23:110–9.",{"doi":1656},"10.1016\u002Fj.tim.2014.10.007",{"id":20,"text":1658,"url":20,"identifiers":1659},"Winn M, Goss RJ, Kimura K, Bugg TD. Antimicrobial nucleoside antibiotics targeting cell wall assembly: recent advances in structure-function studies and nucleoside biosynthesis. Nat Prod Rep. 2010;27:279–304.",{"doi":1660},"10.1039\u002FB816215H",{"id":20,"text":1662,"url":20,"identifiers":1663},"Karwowski JP, Jackson M, Theriault RJ, Chen RH, Barlow GJ, Maus ML. Pacidamycins, a novel series of antibiotics with anti-Pseudomonas aeruginosa activity. I. Taxonomy of the producing organism and fermentation. J Antibiot (Tokyo). 1989;42:506–11.",{"doi":1664},"10.7164\u002Fantibiotics.42.506",{"id":20,"text":1666,"url":20,"identifiers":1667},"Kaysser L, Tang X, Wemakor E, Sedding K, Hennig S, Siebenberg S, Gust B. Identification of a napsamycin biosynthesis gene cluster by genome mining. ChemBioChem. 2011;12:477–87.",{"doi":1668},"10.1002\u002Fcbic.201000460",{"id":20,"text":1670,"url":20,"identifiers":1671},"Li Q, Wang L, Xie Y, Wang S, Chen R, Hong B. SsaA, a member of a novel class of transcriptional regulators, controls sansanmycin production in Streptomyces sp. strain SS through a feedback mechanism. J Bacteriol. 2013;195:2232–43.",{"doi":1672},"10.1128\u002FJB.00054-13",{"id":20,"text":1674,"url":20,"identifiers":1675},"Inukai M, Isono F, Takahashi S, Enokita R, Sakaida Y, Haneishi T. Mureidomycins A-D, novel peptidylnucleoside antibiotics with spheroplast forming activity. I. Taxonomy, fermentation, isolation and physico-chemical properties. J Antibiot (Tokyo). 1989;42:662–6.",{"doi":1676},"10.7164\u002Fantibiotics.42.662",{"id":20,"text":1678,"url":20,"identifiers":1679},"Rackham EJ, Grüschow S, Ragab AE, Dickens S, Goss RJ. Pacidamycin biosynthesis: identification and heterologous expression of the first uridyl peptide antibiotic gene cluster. ChemBioChem. 2010;11:1700–9.",{"doi":1680},"10.1002\u002Fcbic.201000200",{"id":20,"text":1682,"url":20,"identifiers":1683},"Zhang W, Ntai I, Bolla ML, Malcolmson SJ, Kahne D, Kelleher NL, Walsh CT. Nine enzymes are required for assembly of the pacidamycin group of peptidyl nucleoside antibiotics. J Am Chem Soc. 2011;133:5240–3.",{"doi":1684},"10.1021\u002Fja2011109",{"id":20,"text":1686,"url":20,"identifiers":1687},"Zhang W, Ostash B, Walsh CT. Identification of the biosynthetic gene cluster for the pacidamycin group of peptidyl nucleoside antibiotics. Proc Natl Acad Sci U S A. 2010;107:16828–33.",{"doi":1688},"10.1073\u002Fpnas.1011557107",{"id":20,"text":1690,"url":20,"identifiers":1691},"Walsh CT, Zhang W. Chemical logic and enzymatic machinery for biological assembly of peptidyl nucleoside antibiotics. ACS Chem Biol. 2011;6:1000–7.",{"doi":1692},"10.1021\u002Fcb200284p",{"id":20,"text":1694,"url":20,"identifiers":1695},"Ragab AE, Grüschow S, Tromans DR, Goss RJ. Biogenesis of the unique 4’,5’-dehydronucleoside of the uridyl peptide antibiotic pacidamycin. J Am Chem Soc. 2011;133:15288–91.",{"doi":1696},"10.1021\u002Fja206163j",{"id":20,"text":1698,"url":20,"identifiers":1699},"Shi Y, Jiang Z, Lei X, Zhang N, Cai Q, Li Q, Wang L, Si S, Xie Y, Hong B. Improving the N-terminal diversity of sansanmycin through mutasynthesis. Microb Cell Fact. 2016;15:77.",{"doi":1700},"10.1186\u002Fs12934-016-0471-1",{"id":20,"text":1702,"url":20,"identifiers":1703},"Deb Roy A, Grüschow S, Cairns N, Goss RJ. Gene expression enabling synthetic diversification of natural products: chemogenetic generation of pacidamycin analogs. J Am Chem Soc. 2010;132:12243–5.",{"doi":1704},"10.1021\u002Fja1060406",{"id":20,"text":1706,"url":20,"identifiers":1707},"Jiang L, Wang L, Zhang J, Liu H, Hong B, Tan H, Niu G. Identification of novel mureidomycin analogues via rational activation of a cryptic gene cluster in Streptomyces roseosporus NRRL 15998. Sci Rep. 2015;5:14111.",{"doi":1708},"10.1038\u002Fsrep14111",{"id":20,"text":1710,"url":20,"identifiers":1711},"Isono F, Inukai M, Takahashi S, Haneishi T, Kinoshita T, Kuwano H. Mureidomycins A-D, novel peptidylnucleoside antibiotics with spheroplast forming activity. II. Structural elucidation. J Antibiot (Tokyo). 1989;42:667–73.",{"doi":1712},"10.7164\u002Fantibiotics.42.667",{"id":20,"text":1714,"url":20,"identifiers":1715},"Isono F, Sakaida Y, Takahashi S, Kinoshita T, Nakamura T, Inukai M. Mureidomycins E and F, minor components of mureidomycins. J Antibiot (Tokyo). 1993;46:1203–7.",{"doi":1716},"10.7164\u002Fantibiotics.46.1203",{"id":20,"text":1718,"url":20,"identifiers":1719},"Li Y, Yu H, Guan H, Li J, Zhang J, Xiang H, Li J, Tan H. Activation of cryptic antibiotic biosynthetic gene clusters guided by RNA-seq data from both Streptomyces ansochromogenes and ΔwblA. Antibiotics (Basel). 2021;10:1097.",{"doi":1720},"10.3390\u002Fantibiotics10091097",{"id":20,"text":1722,"url":20,"identifiers":1723},"Liu N, Guan H, Niu G, Jiang L, Li Y, Zhang J, Li J, Tan H. Molecular mechanism of mureidomycin biosynthesis activated by introduction of an exogenous regulatory gene ssaA into Streptomyces roseosporus. Sci China Life Sci. 2021;64:1949–63.",{"doi":1724},"10.1007\u002Fs11427-020-1892-3",{"id":20,"text":1726,"url":20,"identifiers":1727},"Kieser T, Bibb MJ, Buttner MJ, Chater KF, Hopwood DA. Practical Streptomyces Genetics. Norwich: John Innes Foundation; 2000.",{},{"id":20,"text":1729,"url":20,"identifiers":1730},"Gregory MA, Till R, Smith MC. Integration site for Streptomyces phage phiBT1 and development of site-specific integrating vectors. J Bacteriol. 2003;185:5320–3.",{"doi":1731},"10.1128\u002FJB.185.17.5320-5323.2003",{"id":1733,"createTime":1734,"updateTime":1735,"relativeEntities":1736,"slug":1737,"properties":1738,"entityType":191,"verifyStatus":192,"verifyTime":1750,"verifyNote":194,"languages":1751,"translateLanguages":1752,"viewCount":21,"primaryUrl":1753,"fullTextUrl":20,"authors":1754,"publicationType":244,"publisherRelationship":1945,"citationCount":21,"citationInfo":1999,"publishDate":20,"publishYear":20,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":2001,"openAccess":20,"references":2002,"isForceReanalyzing":303},"e0eaf988-cd36-45d5-a690-8015e3d18fce","2024-04-21T03:58:54.347+00:00","2026-09-05T07:11:15.381+00:00",[],"Engineering-Streptomyces-sp-CPCC-204095-for-the-targeted-high-level-production-of-isatropolone-A-by-elucidating-its-pathway-specific-regulatory-mechanism",{"openalex":1739,"abstract":1741,"title":1743,"pm":1746,"doi":1748},{"VOID":1740},"W4394853858",{"EN":1742},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:sec>\n                \u003Cjats:title>Background\u003C\u002Fjats:title>\n                \u003Cjats:p>Isatropolone A and C, produced by \u003Cjats:italic>Streptomyces\u003C\u002Fjats:italic> sp. CPCC 204095, belong to an unusual class of non-benzenoid aromatic compounds and contain a rare seven-membered ring structure. Isatropolone A exhibits potent activity against \u003Cjats:italic>Leishmania donovani\u003C\u002Fjats:italic>, comparable to the only oral drug miltefosine. However, its variably low productivity represents a limitation for this lead compound in the future development of new anti-leishmaniasis drugs to meet unmet clinical needs.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>Here we first elucidated the regulatory cascade of biosynthesis of isatropolones, which consists of two SARP family regulators, IsaF and IsaJ. Through a series of in vivo and in vitro experiments, IsaF was identified as a pathway-specific activator that orchestrates the transcription of the gene cluster essential for isatropolone biosynthesis. Interestingly, IsaJ was found to only upregulate the expression of the cytochrome P450 monooxygenase IsaS, which is crucial for the yield and proportion of isatropolone A and C. Through targeted gene deletions of \u003Cjats:italic>isaJ\u003C\u002Fjats:italic> or \u003Cjats:italic>isaS\u003C\u002Fjats:italic>, we effectively impeded the conversion of isatropolone A to C. Concurrently, the facilitation of \u003Cjats:italic>isaF\u003C\u002Fjats:italic> overexpression governed by selected promoters, prompted the comprehensive activation of the production of isatropolone A. Furthermore, meticulous optimization of the fermentation parameters was conducted. These strategies culminated in the attainment of an unprecedented maximum yield—980.8 mg\u002FL of isatropolone A—achieved in small-scale solid-state fermentation utilizing the genetically modified strains, thereby establishing the highest reported titer to date.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusion\u003C\u002Fjats:title>\n                \u003Cjats:p>In \u003Cjats:italic>Streptomyces\u003C\u002Fjats:italic> sp. CPCC 204095, the production of isatropolone A and C is modulated by the SARP regulators IsaF and IsaJ. IsaF serves as a master pathway-specific regulator for the production of isatropolones. IsaJ, on the other hand, only dictates the transcription of IsaS, the enzyme responsible for the conversion of isatropolone A and C. By engineering the expression of these pivotal genes, we have devised a strategy for genetic modification aimed at the selective and high-yield biosynthesis of isatropolone A. This study not only unveils the unique regulatory mechanisms governing isatropolone biosynthesis for the first time, but also establishes an essential engineering framework for the targeted high-level production of isatropolone A.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":1744,"VI":1745},"Engineering Streptomyces sp. CPCC 204095 for the targeted high-level production of isatropolone A by elucidating its pathway-specific regulatory mechanism","Cải biến Streptomyces sp. CPCC 204095 nhằm sản xuất isatropolone A mức độ cao có mục tiêu bằng cách làm sáng tỏ cơ chế điều hòa đặc hiệu con đường",{"VOID":1747},"38622698",{"VOID":1749},"10.1186\u002Fs12934-024-02387-0","2025-02-02T09:44:57.987+00:00",[1144],[196],"https:\u002F\u002Fmicrobialcellfactories.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12934-024-02387-0",[1755,1774,1791,1808,1825,1842,1859,1876,1893,1910,1927],{"id":1756,"sortIndex":21,"researcher":20,"roles":1757,"affiliations":1758,"properties":1767,"displayName":1771,"givenName":20,"familyName":20},"cab03b75-ef14-4a08-a5eb-5dd8ecd73cb9",[],[1759],{"id":1760,"sortIndex":21,"affiliation":1761,"properties":20},"1626d01f-b9ca-4f92-87c6-e3c719b83553",{"id":1760,"createTime":20,"updateTime":20,"relativeEntities":1762,"slug":20,"properties":1763,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1766,"statistic":20},[],{"title":1764},{"EN":1765},"CAMS Key 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H, Roman D, Beemelmanns C. 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Nat Commun. 2016;7:13083.",{"doi":2030},"10.1038\u002Fncomms13083",{"id":20,"text":2032,"url":20,"identifiers":2033},"Cai X, Shi YM, Pöhlmann N, Revermann O, Bahner I, Pidot SJ, Wesche F, Lackner H, Büchel C, Kaiser M, et al. Structure and biosynthesis of isatropolones, bioactive amine-scavenging fluorescent natural products from Streptomyces Gö66. Angew Chem Int Ed Engl. 2017;56:4945–9.",{"doi":2034},"10.1002\u002Fanie.201701223",{"id":20,"text":2036,"url":20,"identifiers":2037},"Guo H, Benndorf R, Leichnitz D, Klassen JL, Vollmers J, Görls H, Steinacker M, Weigel C, Dahse HM, Kaster AK et al. Isolation, biosynthesis and chemical modifications of rubterolones A-F: rare tropolone alkaloids from Actinomadura sp. 5 – 2. Chemistry. 2017;23:9338–45.",{"doi":2038},"10.1002\u002Fchem.201701005",{"id":20,"text":2040,"url":20,"identifiers":2041},"Li L, Li S, Jiang B, Zhang M, Zhang J, Yang B, Li L, Yu L, Liu H, You X, et al. Isarubrolones containing a pyridooxazinium unit from Streptomyces as autophagy activators. J Nat Prod. 2019;82:1149–54.",{"doi":2042},"10.1021\u002Facs.jnatprod.8b00857",{"id":20,"text":2044,"url":20,"identifiers":2045},"Li L, Zhang M, Li S, Jiang B, Zhang J, Yu L, Liu H, Wu L. Isatropolone\u002Fisarubrolone C(m) from Streptomyces with biological activity of inducing incomplete autophagy. J Antibiot (Tokyo). 2022;75:702–8.",{"doi":2046},"10.1038\u002Fs41429-022-00575-x",{"id":20,"text":2048,"url":20,"identifiers":2049},"Ponte-Sucre A, Gamarro F, Dujardin JC, Barrett MP, López-Vélez R, García-Hernández R, Pountain AW, Mwenechanya R, Papadopoulou B. Drug resistance and treatment failure in leishmaniasis: a 21st century challenge. PLoS Negl Trop Dis. 2017;11:e0006052.",{"doi":2050},"10.1371\u002Fjournal.pntd.0006052",{"id":20,"text":2052,"url":20,"identifiers":2053},"Liu X, Li S, Li L, Liu J, Jiang b, Wu L. Solid state fermentation of Streptomyces sp. CPCC 204095 and preparation of isatropolone C. Chin Med Biotechno. 2021;16(4):302–6.",{},{"id":20,"text":2055,"url":20,"identifiers":2056},"Wietzorrek A, Bibb M. A novel family of proteins that regulates antibiotic production in Streptomycetes appears to contain an OmpR-like DNA-binding fold. Mol Microbiol. 1997;25:1181–4.",{"doi":2057},"10.1046\u002Fj.1365-2958.1997.5421903.x",{"id":20,"text":2059,"url":20,"identifiers":2060},"Mast Y, Guezguez J, Handel F, Schinko E. A complex signaling cascade governs pristinamycin biosynthesis in Streptomyces pristinaespiralis. Appl Environ Microbiol. 2015;81:6621–36.",{"doi":2061},"10.1128\u002FAEM.00728-15",{"id":20,"text":2063,"url":20,"identifiers":2064},"Yin S, Wang W, Wang X, Zhu Y, Jia X, Li S, Yuan F, Zhang Y, Yang K. Identification of a cluster-situated activator of oxytetracycline biosynthesis and manipulation of its expression for improved oxytetracycline production in Streptomyces rimosus. Microb Cell Fact. 2015;14:46.",{"doi":2065},"10.1186\u002Fs12934-015-0231-7",{"id":20,"text":2067,"url":20,"identifiers":2068},"Kahmann JD, Sass HJ, Allan MG, Seto H, Thompson CJ, Grzesiek S. Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators. Embo J. 2003;22:1824–34.",{"doi":2069},"10.1093\u002Femboj\u002Fcdg181",{"id":20,"text":2071,"url":20,"identifiers":2072},"Martín JF, Liras P. Engineering of regulatory cascades and networks controlling antibiotic biosynthesis in Streptomyces. Curr Opin Microbiol. 2010;13:263–73.",{"doi":2073},"10.1016\u002Fj.mib.2010.02.008",{"id":20,"text":2075,"url":20,"identifiers":2076},"van Wezel GP, McDowall KJ. The regulation of the secondary metabolism of Streptomyces: new links and experimental advances. Nat Prod Rep. 2011;28:1311–33.",{"doi":2077},"10.1039\u002Fc1np00003a",{"id":20,"text":2079,"url":20,"identifiers":2080},"Sono MRM, Coulter ED, Dawson JH. Heme-containing oxygenases. Chem Rev. 1996;96:2841–88.",{"doi":2081},"10.1021\u002Fcr9500500",{"id":20,"text":2083,"url":20,"identifiers":2084},"Zhao B, Lamb DC, Lei L, Kelly SL, Yuan H, Hachey DL, Waterman MR. Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry. 2007;46:8725–33.",{"doi":2085},"10.1021\u002Fbi7006959",{"id":20,"text":2087,"url":20,"identifiers":2088},"Mendes MV, Recio E, Fouces R, Luiten R, Martín JF, Aparicio JF. Engineered biosynthesis of novel polyenes: a pimaricin derivative produced by targeted gene disruption in Streptomyces Natalensis. Chem Biol. 2001;8:635–44.",{"doi":2089},"10.1016\u002FS1074-5521(01)00033-3",{"id":20,"text":2091,"url":20,"identifiers":2092},"Sarwar A, Latif Z, Zhang S, Zhu J, Zechel DL, Bechthold A. Biological control of potato common scab with rare isatropolone C compound produced by plant growth promoting Streptomyces A1RT. Front Microbiol. 2018;9:1126.",{"doi":2093},"10.3389\u002Ffmicb.2018.01126",{"id":20,"text":2095,"url":20,"identifiers":2096},"Yu Q, Du A, Liu T, Deng Z, He X. The biosynthesis of the polyether antibiotic nanchangmycin is controlled by two pathway-specific transcriptional activators. Arch Microbiol. 2012;194:415–26.",{"doi":2097},"10.1007\u002Fs00203-011-0768-8",{"id":20,"text":2099,"url":20,"identifiers":2100},"Shao Z, Rao G, Li C, Abil Z, Luo Y, Zhao H. Refactoring the silent spectinabilin gene cluster using a plug-and-play scaffold. ACS Synth Biol. 2013;2:662–9.",{"doi":2101},"10.1021\u002Fsb400058n",{"id":20,"text":2103,"url":20,"identifiers":2104},"Wang W, Li X, Wang J, Xiang S, Feng X, Yang K. An engineered strong promoter for streptomycetes. Appl Environ Microbiol. 2013;79:4484–92.",{"doi":2105},"10.1128\u002FAEM.00985-13",{"id":20,"text":2107,"url":20,"identifiers":2108},"Li S, Wang J, Li X, Yin S, Wang W, Yang K. Genome-wide identification and evaluation of constitutive promoters in streptomycetes. Microb Cell Fact. 2015;14:172.",{"doi":2109},"10.1186\u002Fs12934-015-0351-0",{"id":20,"text":2111,"url":20,"identifiers":2112},"Li X, Zhang C, Zhao Y, Lei X, Jiang Z, Zhang X, Zheng Z, Si S, Wang L, Hong B. Comparative genomics and transcriptomics analyses provide insights into the high yield and regulatory mechanism of norvancomycin biosynthesis in Amycolatopsis orientalis NCPC 2–48. Microb Cell Fact. 2021;20:28.",{"doi":2113},"10.1186\u002Fs12934-021-01521-6",{"id":20,"text":2115,"url":20,"identifiers":2116},"Eugene V, Hort P, ;Earl NJ, Williams P. Pen Aegyl, Pa. Process for preparation of quaternized cationic vinyllactam-acrylamide copolymers. Vol. US-4057533-A. Volume 8. USA: GFA Corporation, NEW YORK, N.Y.;; 1977-11-08. p. 8.",{},{"id":20,"text":2118,"url":20,"identifiers":2119},"Kieser T, Bibb MJ, Chater KF, Butter M, Hopwood D, Bittner ML, Buttner MJ. Practical Streptomyces Genetics: A Laboratory Manual. 2000.",{},{"id":20,"text":2121,"url":20,"identifiers":2122},"Hong B, Phornphisutthimas S, Tilley E, Baumberg S, McDowall KJ. Streptomycin production by Streptomyces griseus can be modulated by a mechanism not associated with change in the adpA component of the A-factor cascade. Biotechnol Lett. 2007;29:57–64.",{"doi":2123},"10.1007\u002Fs10529-006-9216-2",{"id":20,"text":2125,"url":20,"identifiers":2126},"Pfaffl MW. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 2001;29:e45.",{"doi":2127},"10.1093\u002Fnar\u002F29.9.e45",{"id":20,"text":2129,"url":20,"identifiers":2130},"Waterhouse A, Bertoni M, Bienert S, Studer G, Tauriello G, Gumienny R, Heer FT, de Beer TAP, Rempfer C, Bordoli L, et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 2018;46:W296–303.",{"doi":2131},"10.1093\u002Fnar\u002Fgky427",{"id":2133,"createTime":2134,"updateTime":2135,"relativeEntities":2136,"slug":2137,"properties":2138,"entityType":191,"verifyStatus":192,"verifyTime":2154,"verifyNote":194,"languages":2155,"translateLanguages":2156,"viewCount":21,"primaryUrl":2157,"fullTextUrl":20,"authors":2158,"publicationType":244,"publisherRelationship":2331,"citationCount":1929,"citationInfo":2384,"publishDate":20,"publishYear":20,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":2386,"openAccess":20,"references":2387,"isForceReanalyzing":303},"27b5e2f8-396d-4982-b506-b130ab554ee2","2024-04-19T14:20:15.782+00:00","2026-09-05T02:12:22.177+00:00",[],"Characterization-of-three-glutamate-decarboxylases-from-Bacillus-spp-for-efficient-%CE%B3-aminobutyric-acid-production",{"mag":2139,"pmc":2141,"openalex":2143,"abstract":2145,"title":2147,"pm":2150,"doi":2152},{"VOID":2140},"3189106252",{"VOID":2142},"8336373",{"VOID":2144},"W3189106252",{"EN":2146},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:sec>\n                \u003Cjats:title>Background\u003C\u002Fjats:title>\n                \u003Cjats:p>Gamma-aminobutyric acid (GABA) is an important bio-product used in pharmaceuticals and functional foods and as a precursor of the biodegradable plastic polyamide 4. Glutamate decarboxylase (GAD) converts \u003Cjats:sc>l\u003C\u002Fjats:sc>-glutamate (\u003Cjats:sc>l\u003C\u002Fjats:sc>-Glu) into GABA via decarboxylation. Compared with other methods, develop a bioconversion platform to produce GABA is of considerable interest for industrial use.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>Three GAD genes were identified from three \u003Cjats:italic>Bacillus\u003C\u002Fjats:italic> strains and heterologously expressed in \u003Cjats:italic>Escherichia coli\u003C\u002Fjats:italic> BL21 (DE3). The optimal reaction temperature and pH values for three enzymes were 40 °C and 5.0, respectively. Of the GADs, GADZ11 had the highest catalytic efficiency towards \u003Cjats:sc>l\u003C\u002Fjats:sc>-Glu (2.19 mM\u003Cjats:sup>− 1\u003C\u002Fjats:sup> s\u003Cjats:sup>− 1\u003C\u002Fjats:sup>). The engineered \u003Cjats:italic>E. coli\u003C\u002Fjats:italic> strain that expressed GADZ11 was used as a whole-cell biocatalyst for the production of GABA. After repeated use 14 times, the cells produced GABA with an average molar conversion rate of 98.6% within 14 h.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusions\u003C\u002Fjats:title>\n                \u003Cjats:p>Three recombinant GADs from \u003Cjats:italic>Bacillus\u003C\u002Fjats:italic> strains have been conducted functional identification. The engineered \u003Cjats:italic>E. coli\u003C\u002Fjats:italic> strain heterologous expressing GADZ1, GADZ11, and GADZ20 could accomplish the biosynthesis of \u003Cjats:sc>l\u003C\u002Fjats:sc>-Glu to GABA in a buffer-free reaction at a high \u003Cjats:sc>l\u003C\u002Fjats:sc>-Glu concentration. The novel engineered \u003Cjats:italic>E. coli\u003C\u002Fjats:italic> strain has the potential to be a cost-effective biotransformation platform for the industrial production of GABA.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":2148,"VI":2149},"Characterization of three glutamate decarboxylases from Bacillus spp. for efficient γ-aminobutyric acid production","Đặc trưng hóa ba glutamate decarboxylase từ Bacillus spp. nhằm sản xuất hiệu quả axit 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