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Annu Rev Microbiol 2004, 58: 521-554. 10.1146\u002Fannurev.micro.57.030502.091022\nDemain AL, Newcomb M, Wu JHD: Cellulase, clostridia, and ethanol. Microbiol Mol Biol Rev 2005, 69: 124-154. 10.1128\u002FMMBR.69.1.124-154.2005\nLynd LR, Van Zyl WH, McBride JE, Laser M: Consolidated bioprocessing of cellulosic biomass: an update. Curr Opin in Biotechnol 2005, 16: 577-583. 10.1016\u002Fj.copbio.2005.08.009\nMcBee RH: The anaerobic thermophilic cellulolytic bacteria. Bacteriol Rev 1950, 14: 51-63.\nMcBee RH: The characteristics of Clostridium thermocellum . J Bacteriol 1954, 67: 505-506.\nSparling R, Islam R, Cicek N, Carere C, Chow H, Levin DB: Formate synthesis by Clostridium thermocellum during anaerobic fermentation. Can J Microbiol 2006, 52: 681-688. 10.1139\u002Fw06-021\nEllis LD, Holwerda EK, Hogsett D, Rogers S, Shao X, Tschaplinski T, Thorne P, Lynd LR: Closing the carbon balance for fermentation by Clostridium thermocellum (ATCC 27405). 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J Food Sci 1987, 52: 1750-1752. 10.1111\u002Fj.1365-2621.1987.tb05926.x\nSnowden MK, Baxter JH, Bergana MM, Reyzer I, Pound V: Stability of N-acetylglutamine and glutamine in aqueous solution and in a liquid nutritional product by an improved HPLC method. J Food Sci 2002, 67: 384-389. 10.1111\u002Fj.1365-2621.2002.tb11415.x\nPark CB, Ryu DDY, Lee SB: Inhibitory effect of L-pyroglutamate on extremophiles: correlation with growth temperature and pH. FEMS Microbiol Lett 2003, 221: 187-190. 10.1016\u002FS0378-1097(03)00213-1\nZhang K, Sawaya MR, Eisenberg DS, Liao JC: Expanding metabolism for biosynthesis of nonnatural alcohols. Proc Natl Acad Sci USA 2008, 105: 20653-20658. 10.1073\u002Fpnas.0807157106\nHigashide W, Li YC, Yang YF, Liao JC: Metabolic engineering of Clostridium cellulolyticum for production of isobutanol from cellulose. Appl Environ Microbiol 2011, 77: 2727-2733. 10.1128\u002FAEM.02454-10\nKanehisa M, Goto S: KEGG: Kyoto Encyclopedia of Genes and Genomes. 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Appl Microbiol Biotechnol 1985, 22: 399-404.\nGuedon E, Payot S, Desvaux M, Petitdemange H: Relationships between cellobiose catabolism, enzyme levels, and metabolic intermediates in Clostridium cellulolyticum grown in a synthetic medium. Biotechnol Bioeng 2000, 67: 327-335. 10.1002\u002F(SICI)1097-0290(20000205)67:3\u003C327::AID-BIT9>3.0.CO;2-U\nDesvaux M, Guedon E, Petitdemange H: Cellulose catabolism by Clostridium cellulolyticum growing in batch culture on defined medium. Appl Environ Microbiol 2000, 66: 2461-2470. 10.1128\u002FAEM.66.6.2461-2470.2000\nGuedon E, Desvaux M, Petitdemange H: Improvement of cellulolytic properties of Clostridium cellulolyticum by metabolic engineering. Appl Environ Microbiol 2002, 68: 53-58. 10.1128\u002FAEM.68.1.53-58.2002\nSaddler JN, Chan MKH: Conversion of pretreated lignocellulosic substrate to ethanol by Clostridium thermocellum in mono-culture and co-culture with Clostridium thermosaccharolyticum and Clostridium thermohydrosulphuricum . Can J Microbiol 1984, 30: 212-220. 10.1139\u002Fm84-032\nVenkateswaran S, Demain AL: The Clostridium thermocellum-Clostridium thermosaccharolyticum ethanol-production process - nutritional studies and scale-down. Chem Eng Commun 1986, 45: 53-60. 10.1080\u002F00986448608911371\nRouwenhorst RJ, Jzn JF, Scheffers WA, Vandijken JP: Determination of protein concentration by total organic -carbon analysis. J Biochem Bioph Methods 1991, 22: 119-128. 10.1016\u002F0165-022X(91)90024-Q\nLi YC, Tschaplinski TJ, Engle NL, Hamilton CY, Rodriguez M, Liao JC, Schadt CW, Guss AM, Yang YF, Graham DE: Combined inactivation of the Clostridium cellulolyticum lactate and malate dehydrogenase genes substantially increases ethanol yield from cellulose and switchgrass fermentations. Biotechnol Biofuels 2012, 5: 13.\nZhang GF, Mortier KA, Storozhenko S, Van De Steene J, Van Der Straeten D, Lambert WE: Free and total para-aminobenzoic acid analysis in plants with high-performance liquid chromatography\u002Ftandem mass spectrometry. Rapid Commun Mass Sp 2005, 19: 963-969. 10.1002\u002Frcm.1878",{"EN":177},"Clostridium thermocellum is a model thermophilic organism for the production of biofuels from lignocellulosic substrates. The majority of publications studying the physiology of this organism use substrate concentrations of ≤10 g\u002FL. However, industrially relevant concentrations of substrate start at 100 g\u002FL carbohydrate, which corresponds to approximately 150 g\u002FL solids. To gain insight into the physiology of fermentation of high substrate concentrations, we studied the growth on, and utilization of high concentrations of crystalline cellulose varying from 50 to 100 g\u002FL by C. thermocellum. Using a defined medium, batch cultures of C. thermocellum achieved 93% conversion of cellulose (Avicel) initially present at 100 g\u002FL. The maximum rate of substrate utilization increased with increasing substrate loading. During fermentation of 100 g\u002FL cellulose, growth ceased when about half of the substrate had been solubilized. However, fermentation continued in an uncoupled mode until substrate utilization was almost complete. In addition to commonly reported fermentation products, amino acids - predominantly L-valine and L-alanine - were secreted at concentrations up to 7.5 g\u002FL. Uncoupled metabolism was also accompanied by products not documented previously for C. thermocellum, including isobutanol, meso- and RR\u002FSS-2,3-butanediol and trace amounts of 3-methyl-1-butanol, 2-methyl-1-butanol and 1-propanol. We hypothesize that C. thermocellum uses overflow metabolism to balance its metabolism around the pyruvate node in glycolysis. C. thermocellum is able to utilize industrially relevant concentrations of cellulose, up to 93 g\u002FL. We report here one of the highest degrees of crystalline cellulose utilization observed thus far for a pure culture of C. thermocellum, the highest maximum substrate utilization rate and the highest amount of isobutanol produced by a wild-type organism.",{"EN":179},"The exometabolome of Clostridium thermocellum reveals overflow metabolism at high cellulose loading",{"VOID":181},"10.1186\u002Fs13068-014-0155-1","PUBLICATION","VERIFIED","Auto Verify","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13068-014-0155-1",[187,204,234,251,267,300,319,338],{"id":188,"sortIndex":189,"researcher":20,"roles":190,"affiliations":192,"properties":201},"eaf873c5-ded4-4e83-9e7e-a02a3d47d842",3,[191],"AUTHOR",[193],{"id":20,"sortIndex":21,"affiliation":194,"properties":20},{"id":195,"createTime":196,"updateTime":196,"relativeEntities":197,"slug":20,"properties":198,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"1581fe25-ea5a-4547-a6d4-ddd47a6c124b","2023-12-12T07:28:00.757+00:00",[],{"title":199},{"VI":200},"Department of Bacteriology, University of Wisconsin-Madison, Madison, USA",{"title":202},{"VI":203},"Daniel Amador-Noguez",{"id":205,"sortIndex":206,"researcher":20,"roles":207,"affiliations":208,"properties":231},"1edd6aa0-d87c-44ca-ac5d-bb5b99ded87b",4,[191],[209,217],{"id":20,"sortIndex":21,"affiliation":210,"properties":20},{"id":211,"createTime":212,"updateTime":212,"relativeEntities":213,"slug":20,"properties":214,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"7d81359e-968e-470c-9926-0adf8bae2c1c","2024-01-12T16:00:35.854+00:00",[],{"title":215},{"VI":216},"nBioEnergy Science Center, Oak Ridge, USA",{"id":218,"sortIndex":219,"affiliation":220,"properties":228},"17d7d093-06d5-4d12-afda-ae795c977809",1,{"id":221,"createTime":222,"updateTime":222,"relativeEntities":223,"slug":224,"properties":225,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"bcaa1691-3bcb-4b69-821a-7864cf9175dc","2024-04-09T23:05:05.818+00:00",[],"Biosciences-Division-Oak-Ridge-National-Laboratory-Oak-Ridge-United-States",{"title":226},{"EN":227},"Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, United States",{"title":229},{"VI":230},"Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, USA",{"title":232},{"VI":233},"Nancy L Engle",{"id":235,"sortIndex":219,"researcher":20,"roles":236,"affiliations":237,"properties":248},"a89dc920-d38f-45a3-ae62-6bdc3b64ff12",[191],[238],{"id":20,"sortIndex":21,"affiliation":239,"properties":20},{"id":240,"createTime":241,"updateTime":242,"relativeEntities":243,"slug":244,"properties":245,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"950443a2-79e9-4a7a-850f-8def1784edf0","2023-12-13T05:51:49.225+00:00","2025-01-04T17:37:14.659+00:00",[],"Mascoma-Corporation-Lebanon-USA",{"title":246},{"VI":247},"Mascoma Corporation, Lebanon, USA",{"title":249},{"VI":250},"Philip G Thorne",{"id":252,"sortIndex":253,"researcher":20,"roles":254,"affiliations":255,"properties":264},"e16b1459-60d2-4eb3-85d0-d1a5665bf5ba",6,[191],[256],{"id":20,"sortIndex":21,"affiliation":257,"properties":20},{"id":258,"createTime":259,"updateTime":259,"relativeEntities":260,"slug":20,"properties":261,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"83983586-6b4b-49b9-97c2-e996e19b41e2","2024-01-12T16:00:35.921+00:00",[],{"title":262},{"VI":263},"Emeritus Industrial Biotechnology of Delft University of Technology, Delft, The Netherlands",{"title":265},{"VI":266},"Johannes P van Dijken",{"id":268,"sortIndex":269,"researcher":20,"roles":270,"affiliations":271,"properties":297},"138bdf83-9513-48a9-9bcd-e4e5a77251b3",7,[191],[272,279,287],{"id":273,"sortIndex":219,"affiliation":274,"properties":278},"34f66bd6-e47f-4121-9a16-b8911a15e0f1",{"id":211,"createTime":212,"updateTime":212,"relativeEntities":275,"slug":20,"properties":276,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":277},{"VI":216},{},{"id":280,"sortIndex":281,"affiliation":282,"properties":286},"3f1f5bbc-dbdd-4334-9d64-f9daf89acd1d",2,{"id":240,"createTime":241,"updateTime":242,"relativeEntities":283,"slug":244,"properties":284,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":285},{"VI":247},{},{"id":20,"sortIndex":21,"affiliation":288,"properties":20},{"id":289,"createTime":290,"updateTime":291,"relativeEntities":292,"slug":293,"properties":294,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"b20ed46b-32e7-4e00-8702-337c1d7f0b2b","2023-12-30T20:51:05.686+00:00","2024-09-23T20:44:19.527+00:00",[],"Thayer-School-of-Engineering-Dartmouth-College-Hanover-USA",{"title":295},{"VI":296},"Thayer School of Engineering, Dartmouth College, Hanover, USA",{"title":298},{"VI":299},"Lee R Lynd",{"id":301,"sortIndex":21,"researcher":20,"roles":302,"affiliations":303,"properties":316},"7b7bd308-b9a0-41db-b705-2af0d041a9f3",[191],[304,309],{"id":20,"sortIndex":21,"affiliation":305,"properties":20},{"id":289,"createTime":290,"updateTime":291,"relativeEntities":306,"slug":293,"properties":307,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":308},{"VI":296},{"id":310,"sortIndex":219,"affiliation":311,"properties":315},"a699bf1b-80e3-4683-850d-3f0f796e333b",{"id":211,"createTime":212,"updateTime":212,"relativeEntities":312,"slug":20,"properties":313,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":314},{"VI":216},{},{"title":317},{"VI":318},"Evert K Holwerda",{"id":320,"sortIndex":281,"researcher":20,"roles":321,"affiliations":322,"properties":335},"2d4da8e0-229a-4970-89b9-69e020addc8c",[191],[323,330],{"id":324,"sortIndex":219,"affiliation":325,"properties":329},"58df9aab-08e2-495b-a2d5-910fe9ea1096",{"id":211,"createTime":212,"updateTime":212,"relativeEntities":326,"slug":20,"properties":327,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":328},{"VI":216},{},{"id":20,"sortIndex":21,"affiliation":331,"properties":20},{"id":289,"createTime":290,"updateTime":291,"relativeEntities":332,"slug":293,"properties":333,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":334},{"VI":296},{"title":336},{"VI":337},"Daniel G Olson",{"id":339,"sortIndex":340,"researcher":20,"roles":341,"affiliations":342,"properties":356},"bee76dc8-4473-43b2-bff4-ea7764932bd2",5,[191],[343,348],{"id":20,"sortIndex":21,"affiliation":344,"properties":20},{"id":211,"createTime":212,"updateTime":212,"relativeEntities":345,"slug":20,"properties":346,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":347},{"VI":216},{"id":349,"sortIndex":219,"affiliation":350,"properties":354},"3f0ce055-1f79-4cb0-af69-5bb0b7d54d79",{"id":221,"createTime":222,"updateTime":222,"relativeEntities":351,"slug":224,"properties":352,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":353},{"EN":227},{"title":355},{"VI":230},{"title":357},{"VI":358},"Timothy J Tschaplinski","ARTICLE",{"url":185,"publisher":361,"properties":382},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":362,"slug":10,"properties":363,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":367,"manageAffiliations":368,"indexDatabases":369,"url":20,"thumbnailPath":20,"statistic":377,"gsStatistic":20,"type":162,"analyzePriority":20},[],{"issn":364,"title":365,"url":366},{"VOID":13},{"EN":15},{"VOID":17},[],[],[370],{"id":78,"indexDatabase":371,"url":91,"indexYears":92,"academicFieldIds":376,"indexDatabaseRanking":99},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":372,"label":373,"description":374,"key":88,"publicationTags":375,"standard":20},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97,98],{"impactFactor":21,"impactFactorByYear":378,"i10Index":112,"i10IndexLast5Year":113,"totalPublication":114,"totalPublicationByYear":379,"totalCitation":129,"totalCitationByYear":380,"totalCitationPerPublication":145,"totalCitationPerPublicationByYear":381,"hindexLast5Year":161,"hindex":161},{"2012":102,"2013":103,"2014":103,"2015":104,"2016":105,"2017":106,"2018":107,"2019":108,"2020":109,"2021":104,"2022":110,"2023":111},{"2008":116,"2009":117,"2010":118,"2011":119,"2012":120,"2013":121,"2014":122,"2015":123,"2016":124,"2017":125,"2018":126,"2019":127,"2020":123,"2021":128},{"2008":131,"2009":132,"2010":133,"2011":134,"2012":135,"2013":136,"2014":137,"2015":138,"2016":139,"2017":140,"2018":141,"2019":142,"2020":143,"2021":144},{"2008":147,"2009":148,"2010":149,"2011":150,"2012":151,"2013":152,"2014":153,"2015":154,"2016":155,"2017":156,"2018":157,"2019":158,"2020":159,"2021":160},{"volume":383,"pages":385},{"VOID":384},"7",{"VOID":386},"1-11","2014-10-21",2014,false,{"id":391,"createTime":392,"updateTime":393,"relativeEntities":394,"slug":395,"properties":396,"entityType":182,"verifyStatus":183,"verifyTime":393,"verifyNote":184,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":405,"fullTextUrl":20,"authors":406,"publicationType":359,"publisherRelationship":517,"citationCount":20,"citationInfo":20,"publishDate":544,"publishYear":545,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":389},"f439685b-0cc2-4048-81af-dfd4c54c637a","2023-12-09T02:54:19.048+00:00","2024-09-15T23:59:25.824+00:00",[],"Enhanced-xylitol-production-using-non-detoxified-xylose-rich-pre-hydrolysate-from-sugarcane-bagasse-by-newly-isolated-Pichia-fermentans",{"references":397,"abstract":399,"title":401,"doi":403},{"VOID":398},"Kwak S, Jo JH, Yun EJ, Jin YS, Seo JH. Production of biofuels and chemicals from xylose using native and engineered yeast strains. Biotechnol Adv. 2019;37:271–83.\nBomble YJ, Lin CY, Amore A, Wei H, Holwerda EK, Ciesielski PN, et al. Lignocellulose deconstruction in the biosphere. Curr Opin Chem Biol. 2017;41:61–70.\nGeng W, Venditti RA, Pawlak JJ, De Assis T, Gonzalez RW, Phillips RB, et al. Techno-economic analysis of hemicellulose extraction from different types of lignocellulosic feedstocks and strategies for cost optimization. Biofuels Bioprod Biorefining. 2020;14:225–41.\nMaio D Di, Turley D. NNFCC. www.nnfcc.co.uk.\nTurley D. A review of the Integrated Biorefining Research and Technology Club (IBTI Club) A report for the Biotechnology and Biological Sciences Research Council (BBSRC) Reviewer. 2017. www.nnfcc.co.uk\nPrabhu AA, Ledesma-Amaro R, Lin CSK, Coulon F, Thakur VK, Kumar V. Bioproduction of succinic acid from xylose by engineered Yarrowia lipolytica without pH control. Biotechnol Biofuels. 2020;13:113.\nSievert C, Nieves LM, Panyon LA, Loeffler T, Morris C, Cartwright RA, et al. Experimental evolution reveals an effective avenue to release catabolite repression via mutations in XylR. Proc Natl Acad Sci USA. 2017;114:7349–54.\nSolarte-Toro JC, Romero-García JM, Martínez-Patiño JC, Ruiz-Ramos E, Castro-Galiano E, Cardona-Alzate CA. Acid pretreatment of lignocellulosic biomass for energy vectors production: a review focused on operational conditions and techno-economic assessment for bioethanol production. Renew Sustain Energy Rev. 2019;1(107):587–601.\nYang B, Tao L, Wyman CE. Strengths, challenges, and opportunities for hydrothermal pretreatment in lignocellulosic biorefineries. Biofuels Bioprod Biorefin. 2018;12(1):125–38.\nCavka A, Jönsson LJ. Detoxification of lignocellulosic hydrolysates using sodium borohydride. Bioresour Technol. 2013;136:368–76.\nChandel AK, da Silva SS, Singh OV. Detoxification of lignocellulose hydrolysates: biochemical and metabolic engineering toward white biotechnology. Bioenergy Res. 2013;6:388–401.\nJönsson LJ, Alriksson B, Nilvebrant NO. Bioconversion of lignocellulose: inhibitors and detoxification. Biotechnol Biofuels. 2013;6:16.\nDasgupta D, Bandhu S, Adhikari DK, Ghosh D. Challenges and prospects of xylitol production with whole cell bio-catalysis: a review. Microbiol Res. 2017;197:9–21.\nFelipe Hernández-Pérez A, de Arruda PV, Sene L, da Silva SS, Kumar Chandel A, de Almeida Felipe MDG. Xylitol bioproduction: state-of-the-art, industrial paradigm shift, and opportunities for integrated biorefineries. Crit Rev Biotechnol. 2019;39:924–43.\nDe Albuquerque TL, Da Silva IJ, De MacEdo GR, Rocha MVP. Biotechnological production of xylitol from lignocellulosic wastes: a review. Process Biochem. 2014;49:1779–89.\nArcaño YD, García ODV, Mandelli D, Carvalho WA, Pontes LAM. Xylitol: a review on the progress and challenges of its production by chemical route. Catal Today. 2020;344:2–14.\nAhmad M, Hirz M, Pichler H, Schwab H. Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production. Appl Microbiol Biotechnol. 2014;98:5301–17.\nSanna ML, Zara S, Zara G, Migheli Q, Budroni M, Mannazzu I. Pichia fermentans dimorphic changes depend on the nitrogen source. Fungal Biol. 2012;116:769–77.\nHuang CF, Jiang YF, Guo GL, Hwang WS. Development of a yeast strain for xylitol production without hydrolysate detoxification as part of the integration of co-product generation within the lignocellulosic ethanol process. Bioresour Technol. 2011;102:3322–9.\nAgbogbo FK, Coward-Kelly G, Torry-Smith M, Wenger KS. Fermentation of glucose\u002Fxylose mixtures using Pichia stipitis. Process Biochem. 2006;41:2333–6.\nOh DK, Kim SY. Increase of xylitol yield by feeding xylose and glucose in Candida tropicalis. Appl Microbiol Biotechnol. 1998;50(4):419–25.\nPal M, Sharma RK. Exoelectrogenic response of Pichia fermentans influenced by mediator and reactor design. J Biosci Bioeng. 2019;127:714–20.\nRossi SC, Medeiros ABP, Weschenfelder TA, de Paula SA, Soccol CR. Use of pervaporation process for the recovery of aroma compounds produced by P. fermentans in sugarcane molasses. Bioprocess Biosyst Eng. 2017;40:959–67.\nKim J-SS, Park J-BB, Jang S-WW, Ha S-JJ. Enhanced xylitol production by mutant Kluyveromyces marxianus 36907-FMEL1 due to improved xylose reductase activity. Appl Biochem Biotechnol. 2015;176:1975–84.\nPal S, Choudhary V, Kumar A, Biswas D, Mondal AK, Sahoo DK. Studies on xylitol production by metabolic pathway engineered Debaryomyces hansenii. Bioresour Technol. 2013;147:449–55.\nGírio FM, Roseiro JCC, Sá-Machado P, Duarte-Reis ARR, Amaral-Collaço MTT. Effect of oxygen transfer rate on levels of key enzymes of xylose metabolism in Debaryomyces hansenii. Enzyme Microb Technol. 1994;16:1074–8.\nWalfridsson M, Anderlund M, Bao X, Hahn-Hägerdal B. Expression of different levels of enzymes from the Pichia stipitis XYL1 and XYL2 genes in Saccharomyces cerevisiae and its effects on product formation during xylose utilisation. Appl Microbiol Biotechnol. 1997;48:218–24.\nCheng K-K, Zhang J-A, Ling H-Z, Ping W-X, Huang W, Ge J-P, et al. Optimization of pH and acetic acid concentration for bioconversion of hemicellulose from corncobs to xylitol by Candida tropicalis. Biochem Eng J. 2009;43:203–7.\nCarvalho GB, Mussatto SI, Cândido EJ, Almeida e Silva JB. Comparison of different procedures for the detoxification of eucalyptus hemicellulosic hydrolysate for use in fermentative processes. J Chem Technol Biotechnol. 2006;81:152–7.\nKim SY, Kim JH, Oh DK. Improvement of xylitol production by controlling oxygen-supply in Candida parapsilosis. J Ferment Bioeng. 1997;83:267–70.\nMussatto SI, Roberto IC. Xylitol production from high xylose concentration: evaluation of the fermentation in bioreactor under different stirring rates. J Appl Microbiol. 2003;95:331–7.\nRoberto IC, Sato S, De Mancilha IM. Effect of inoculum level on xylitol production from rice straw hemicellulose hydrolysate by Candida guilliermondii. J Ind Microbiol. 1996;16:348–50.\nUnrean P, Ketsub N. Integrated lignocellulosic bioprocess for co-production of ethanol and xylitol from sugarcane bagasse. Ind Crops Prod. 2018;123:238–46.\nZhang J, Geng A, Yao C, Lu Y, Li Q. Xylitol production from d-xylose and horticultural waste hemicellulosic hydrolysate by a new isolate of Candida athensensis SB18. Bioresour Technol. 2012;105:134–41.\nLing H, Cheng K, Ge J, Ping W. Statistical optimization of xylitol production from corncob hemicellulose hydrolysate by Candida tropicalis HDY-02. N Biotechnol. 2011;28:673–8.\nYewale T, Panchwagh S, Sawale S, Jain R, Dhamole PB. Xylitol production from non-detoxified and non-sterile lignocellulosic hydrolysate using low-cost industrial media components. 3 Biotech. 2017;7:68.\nRodrigues RCLB, Felipe MGA, Roberto IC, Vitolo M. Batch xylitol production by Candida guilliermondii FTI 20037 from sugarcane bagasse hemicellulosic hydrolyzate at controlled pH values. Bioprocess Biosyst Eng. 2003;26:103–7.\nSilva SS, Roberto IC, Felipe MGA, Mancilha IM. Batch fermentation of xylose for xylitol production in stirred tank bioreactor. Process Biochem. 1996;31:549–53.\nFaria LFF, Gimenes MAP, Nobrega R, Pereira N. Influence of oxygen availability on cell growth and xylitol production by Candida guilliermondii. In: Biotechnol Fuels Chem. 2002; pp. 449–58.\nWalther T, Hensirisak P, Agblevor FA. The influence of aeration and hemicellulosic sugars on xylitol production by Candida tropicalis. Bioresour Technol. 2001;76:213–20.\nPrabhu AA, Gadela R, Bharali B, Deshavath NN, Dasu VV. Development of high biomass and lipid yielding medium for newly isolated Rhodotorula mucilaginosa. Fuel. 2019;239:874–85.\nCheng KK, Ling HZ, Zhang JA, Ping WX, Huang W, Ge JP, et al. Strain isolation and study on process parameters for xylose-to-xylitol byconversion. Biotechnol Biotechnol Equip. 2010;24:1606–11.\nWinston F. EMS and UV mutagenesis in yeast. Curr Protoc Mol Bio. 2008;82:13.3B.1–13.3B.5.\nPrabhu AA, Thomas DJ, Ledesma-Amaro R, Leeke GA, Medina A, Verheecke-Vaessen C, et al. Biovalorisation of crude glycerol and xylose into xylitol by oleaginous yeast Yarrowia lipolytica. Microb Cell Fact. 2020;19:121.\nPrabhu AA, Mandal B, Dasu VV. Medium optimization for high yield production of extracellular human interferon-γ from Pichia pastoris: a statistical optimization and neural network-based approach. Korean J Chem Eng. 2017;34:110–1121.\nKo BS, Kim JHJ, Kim JHJ. Production of xylitol from D-xylose by a xylitol dehydrogenase gene-disrupted mutant of Candida tropicalis. Appl Environ Microbiol. 2006;72:4207–13.\nPrakash G, Varma AJ, Prabhune A, Shouche Y, Rao M. Microbial production of xylitol from D-xylose and sugarcane bagasse hemicellulose using newly isolated thermotolerant yeast Debaryomyces hansenii. Bioresour Technol. 2011;102:3304–8.\nSu B, Wu M, Zhang Z, Lin J, Yang L. Efficient production of xylitol from hemicellulosic hydrolysate using engineered Escherichia coli. Metab Eng. 2015;31:112–22.\nRodrigues RCLB, Kenealy WR, Jeffries TW. Xylitol production from DEO hydrolysate of corn stover by Pichia stipitis YS-30. J Ind Microbiol Biotechnol. 2011;38:1649–55.\nZhang J, Zhang B, Wang D, Gao X, Hong J. Xylitol production at high temperature by engineered Kluyveromyces marxianus. Bioresour Technol. 2014;152:192–201.",{"EN":400},"Integrated management of hemicellulosic fraction and its economical transformation to value-added products is the key driver towards sustainable lignocellulosic biorefineries. In this aspect, microbial cell factories are harnessed for the sustainable production of commercially viable biochemicals by valorising C5 and C6 sugars generated from agro-industrial waste. However, in the terrestrial ecosystem, microbial systems can efficiently consume glucose. On the contrary, pentose sugars are less preferred carbon source as most of the microbes lack metabolic pathway for their utilization. The effective utilization of both pentose and hexose sugars is key for economical biorefinery. Bioprospecting the food waste and selective enrichment on xylose-rich medium led to screening and isolation of yeast which was phylogenetically identified as Pichia fermentans. The newly isolated xylose assimilating yeast was explored for xylitol production. The wild type strain robustly grew on xylose and produced xylitol with > 40% conversion yield. Chemical mutagenesis of isolated yeast with ethyl methanesulphonate (EMS) yielded seven mutants. The mutant obtained after 15 min EMS exposure, exhibited best xylose bioconversion efficiency. This mutant under shake flask conditions produced maximum xylitol titer and yield of 34.0 g\u002FL and 0.68 g\u002Fg, respectively. However, under the same conditions, the control wild type strain accumulated 27.0 g\u002FL xylitol with a conversion yield of 0.45 g\u002Fg. Improved performance of the mutant was attributed to 34.6% activity enhancement in xylose reductase with simultaneous reduction of xylitol dehydrogenase activity by 22.9%. Later, the culture medium was optimized using statistical design and validated at shake flask and bioreactor level. Bioreactor studies affirmed the competence of the mutant for xylitol accumulation. The xylitol titer and yield obtained with pure xylose were 98.9 g\u002FL and 0.67 g\u002Fg, respectively. In comparison, xylitol produced using non-detoxified xylose rich pre-hydrolysate from sugarcane bagasse was 79.0 g\u002FL with an overall yield of 0.54 g\u002Fg. This study demonstrates the potential of newly isolated P. fermentans in successfully valorising the hemicellulosic fraction for the sustainable xylitol production.",{"EN":402},"Enhanced xylitol production using non-detoxified xylose rich pre-hydrolysate from sugarcane bagasse by newly isolated Pichia fermentans",{"VOID":404},"10.1186\u002Fs13068-020-01845-2","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13068-020-01845-2",[407,422,437,452,469,481,493,505],{"id":408,"sortIndex":189,"researcher":20,"roles":409,"affiliations":410,"properties":419},"c0d336b9-ddb6-4c25-be29-1ac19c976f68",[191],[411],{"id":20,"sortIndex":21,"affiliation":412,"properties":20},{"id":413,"createTime":414,"updateTime":414,"relativeEntities":415,"slug":20,"properties":416,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"d950e8fd-1dd1-4aed-a8a9-1ada2677c52e","2023-12-09T02:53:32.718+00:00",[],{"title":417},{"VI":418},"Biochemistry and Biotechnology Area, Material Resource Efficiency Division, CSIR-Indian Institute of Petroleum, Mohkampur, Dehradun, India",{"title":420},{"VI":421},"Deepti Agrawal",{"id":423,"sortIndex":340,"researcher":20,"roles":424,"affiliations":425,"properties":434},"33c08b76-81e2-41cb-a493-fc6e242efb38",[191],[426],{"id":20,"sortIndex":21,"affiliation":427,"properties":20},{"id":428,"createTime":429,"updateTime":429,"relativeEntities":430,"slug":20,"properties":431,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"79cda99a-9916-4c0e-9ac8-d2c8bbfe3ef9","2023-12-09T02:54:19.100+00:00",[],{"title":432},{"VI":433},"Centre for Energy and Environment, Malaviya National Institute of Technology, Jaipur, India",{"title":435},{"VI":436},"Vivekanand Vivekanand",{"id":438,"sortIndex":219,"researcher":20,"roles":439,"affiliations":440,"properties":449},"b8a56c52-7585-4d64-b461-e8be9a8daf11",[191],[441],{"id":20,"sortIndex":21,"affiliation":442,"properties":20},{"id":443,"createTime":444,"updateTime":444,"relativeEntities":445,"slug":20,"properties":446,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"68571757-5e37-4638-b24c-856072243ef3","2023-12-09T02:53:32.757+00:00",[],{"title":447},{"VI":448},"School of Water, Energy and Environment, Cranfield University, Cranfield, UK",{"title":450},{"VI":451},"Ekkarin Bosakornranut",{"id":453,"sortIndex":253,"researcher":20,"roles":454,"affiliations":455,"properties":466},"d9c1fe28-f42a-4fe8-8a48-6ed49c9c6a84",[191],[456],{"id":20,"sortIndex":21,"affiliation":457,"properties":20},{"id":458,"createTime":459,"updateTime":460,"relativeEntities":461,"slug":462,"properties":463,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"9206b36c-3912-4548-a850-4a927cf1ef29","2023-12-09T02:54:19.112+00:00","2024-09-04T19:37:24.327+00:00",[],"Biorefining-and-Advanced-Materials-Research-Centre-Scotland-s-Rural-College-SRUC-Edinburgh-UK",{"title":464},{"VI":465},"Biorefining and Advanced Materials Research Centre, Scotland’s Rural College (SRUC), Edinburgh, UK",{"title":467},{"VI":468},"Vijay Kumar Thakur",{"id":470,"sortIndex":21,"researcher":20,"roles":471,"affiliations":472,"properties":478},"7abde74b-b7a0-4128-8501-5467500fb32f",[191],[473],{"id":20,"sortIndex":21,"affiliation":474,"properties":20},{"id":443,"createTime":444,"updateTime":444,"relativeEntities":475,"slug":20,"properties":476,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":477},{"VI":448},{"title":479},{"VI":480},"Ashish A. 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Although oxidoreductases that oxidize cellulosic hydrolysates have been well characterized, none have been reported to oxidize substituted or branched xylo-oligosaccharides. Moreover, this is the first report that identifies amino acid substitutions leading to GOOX variants with reduced substrate inhibition.\u003C\u002Fjats:p>\n          \u003C\u002Fjats:sec>\n          \u003Cjats:sec>\n            \u003Cjats:title>Results\u003C\u002Fjats:title>\n            \u003Cjats:p>The recombinant wild type gluco-oligosaccharide oxidase (GOOX) from the fungus \u003Cjats:italic>Sarocladium strictum\u003C\u002Fjats:italic>, along with variants that were generated by site-directed mutagenesis, retained the FAD cofactor, and showed high activity on cello-oligosaccharide and xylo-oligosaccharides, including substituted and branched xylo-oligosaccharides. Mass spectrometric analyses confirmed that GOOX introduces one oxygen atom to oxidized products, and \u003Cjats:sup>1\u003C\u002Fjats:sup>H NMR and tandem mass spectrometry analysis confirmed that oxidation was restricted to the anomeric carbon. The A38V mutation, which is close to a predicted divalent ion-binding site in the FAD-binding domain of GOOX but 30 Å away from the active site, significantly increased the \u003Cjats:italic>k\u003C\u002Fjats:italic>\n              \u003Cjats:sub>cat\u003C\u002Fjats:sub> and catalytic efficiency of the enzyme on all oligosaccharides. Eight amino acid substitutions were separately introduced to the substrate-binding domain of GOOX-VN (at positions Y72, E247, W351, Q353 and Q384). In all cases, the \u003Cjats:italic>K\u003C\u002Fjats:italic>\n              \u003Cjats:sub>m\u003C\u002Fjats:sub> of the enzyme variant was higher than that of GOOX, supporting the role of corresponding residues in substrate binding. Most notably, W351A increased \u003Cjats:italic>K\u003C\u002Fjats:italic>\n              \u003Cjats:sub>m\u003C\u002Fjats:sub> values by up to two orders of magnitude while also increasing \u003Cjats:italic>k\u003C\u002Fjats:italic>\n              \u003Cjats:sub>cat\u003C\u002Fjats:sub> up to 3-fold on cello- and xylo-oligosaccharides and showing no substrate inhibition.\u003C\u002Fjats:p>\n          \u003C\u002Fjats:sec>\n          \u003Cjats:sec>\n            \u003Cjats:title>Conclusions\u003C\u002Fjats:title>\n            \u003Cjats:p>This study provides further evidence that \u003Cjats:italic>S\u003C\u002Fjats:italic>. \u003Cjats:italic>strictum\u003C\u002Fjats:italic> GOOX has broader substrate specificity than the enzyme name implies, and that substrate inhibition can be reduced by removing aromatic side chains in the -2 binding subsite. Of the enzyme variants, W351A might be particularly advantageous when oxidizing oligosaccharides present at high substrate concentrations often experienced in industrial processes.\u003C\u002Fjats:p>\n          \u003C\u002Fjats:sec>",{"EN":563},"Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictumand variants with reduced substrate inhibition",{"VOID":565},"24119501",{"VOID":567},"10.1186\u002F1754-6834-6-148",[569],"EN","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002F1754-6834-6-148",[572,591,611,628,647,664,681],{"id":573,"sortIndex":189,"researcher":20,"roles":574,"affiliations":575,"properties":586},"925a64f5-196f-4886-95b6-200e7ed892df",[],[576],{"id":577,"sortIndex":21,"affiliation":578,"properties":20},"95330e07-754d-44ff-a32e-4edf05f1b943",{"id":579,"createTime":580,"updateTime":580,"relativeEntities":581,"slug":582,"properties":583,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"3bfd1513-9fad-4313-94b1-3c0de39524a4","2024-04-19T11:34:06.551+00:00",[],"Department-of-Food-and-Environmental-Sciences-University-of-Helsinki-P-O-Box-27-Helsinki-00014-Finland",{"title":584},{"EN":585},"Department of Food and Environmental Sciences, University of Helsinki, P.O. 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Appl Biochem Biotechnol. 1990, 24: 1-14. 10.1007\u002FBF02920229.",{"EN":1239},"Mineral elements present in lignocellulosic biomass feedstocks may accumulate in biorefinery process streams and cause technological problems, or alternatively can be reaped for value addition. A better understanding of the distribution of minerals in biomass in response to pretreatment factors is therefore important in relation to development of new biorefinery processes. The objective of the present study was to examine the levels of mineral elements in pretreated wheat straw in response to systematic variations in the hydrothermal pretreatment parameters (pH, temperature, and treatment time), and to assess whether it is possible to model mineral levels in the pretreated fiber fraction. Principal component analysis of the wheat straw biomass constituents, including mineral elements, showed that the recovered levels of wheat straw constituents after different hydrothermal pretreatments could be divided into two groups: 1) Phosphorus, magnesium, potassium, manganese, zinc, and calcium correlated with xylose and arabinose (that is, hemicellulose), and levels of these constituents present in the fiber fraction after pretreatment varied depending on the pretreatment-severity; and 2) Silicon, iron, copper, aluminum correlated with lignin and cellulose levels, but the levels of these constituents showed no severity-dependent trends. For the first group, an expanded pretreatment-severity equation, containing a specific factor for each constituent, accounting for variability due to pretreatment pH, was developed. Using this equation, the mineral levels could be predicted with R2 > 0.75; for some with R2 up to 0.96. Pretreatment conditions, especially pH, significantly influenced the levels of phosphorus, magnesium, potassium, manganese, zinc, and calcium in the resulting fiber fractions. A new expanded pretreatment-severity equation is proposed to model and predict mineral composition in pretreated wheat straw biomass.",{"EN":1241},"Biorefining of wheat straw: accounting for the distribution of mineral elements in pretreated biomass by an extended pretreatment-severity equation",{"VOID":1243},"10.1186\u002Fs13068-014-0141-7","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13068-014-0141-7",[1246,1262,1277,1301,1313],{"id":1247,"sortIndex":189,"researcher":20,"roles":1248,"affiliations":1249,"properties":1259},"179c0e95-80eb-418c-b210-bd5467465bad",[191],[1250],{"id":20,"sortIndex":21,"affiliation":1251,"properties":20},{"id":1252,"createTime":1253,"updateTime":1253,"relativeEntities":1254,"slug":1255,"properties":1256,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"f0637ff1-84a3-4b6b-a29b-2cc426e8c787","2024-04-14T21:58:19.424+00:00",[],"Plant-and-Soil-Science-Section-Department-of-Plant-and-Environmental-Sciences-Faculty-of-Science-University-of-Copenhagen-Frederiksberg-C-Denmark",{"title":1257},{"EN":1258},"Plant and Soil Science Section, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Frederiksberg C, Denmark",{"title":1260},{"VI":1261},"Jan K Schjoerring",{"id":1263,"sortIndex":281,"researcher":20,"roles":1264,"affiliations":1265,"properties":1274},"9792c79b-50f5-40cd-b2d5-4a641751ba08",[191],[1266],{"id":20,"sortIndex":21,"affiliation":1267,"properties":20},{"id":1268,"createTime":1269,"updateTime":1269,"relativeEntities":1270,"slug":20,"properties":1271,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"7e88ea59-20d6-4b75-951e-82425df2dd2f","2024-01-08T15:40:53.610+00:00",[],{"title":1272},{"VI":1273},"DONG Energy, Fredericia, Denmark",{"title":1275},{"VI":1276},"Niels Ole Knudsen",{"id":1278,"sortIndex":21,"researcher":20,"roles":1279,"affiliations":1280,"properties":1298},"81ffa3a9-0e29-4386-843d-cc9b63b58bfe",[191],[1281,1293],{"id":1282,"sortIndex":219,"affiliation":1283,"properties":1292},"bcb8499e-000d-4ac0-80d3-0864a0b609a9",{"id":1284,"createTime":1285,"updateTime":1286,"relativeEntities":1287,"slug":1288,"properties":1289,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"0c929e4d-6f35-4375-82f2-c3b71bee354e","2023-12-28T15:47:13.095+00:00","2025-06-12T01:23:15.693+00:00",[],"Center-for-Bioprocess-Engineering-Department-of-Chemical-and-Biochemical-Engineering-Technical-University-of-Denmark-Lyngby-Denmark",{"title":1290},{"VI":1291},"Center for Bioprocess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark, Lyngby, Denmark",{},{"id":20,"sortIndex":21,"affiliation":1294,"properties":20},{"id":1268,"createTime":1269,"updateTime":1269,"relativeEntities":1295,"slug":20,"properties":1296,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1297},{"VI":1273},{"title":1299},{"VI":1300},"Duy Michael Le",{"id":1302,"sortIndex":206,"researcher":20,"roles":1303,"affiliations":1304,"properties":1310},"56f1ae66-2fec-4a1f-ac68-4c6cf1a0dac2",[191],[1305],{"id":20,"sortIndex":21,"affiliation":1306,"properties":20},{"id":1284,"createTime":1285,"updateTime":1286,"relativeEntities":1307,"slug":1288,"properties":1308,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1309},{"VI":1291},{"title":1311},{"VI":1312},"Anne S 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Sørensen",{"url":1244,"publisher":1326,"properties":1347},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1327,"slug":10,"properties":1328,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1332,"manageAffiliations":1333,"indexDatabases":1334,"url":20,"thumbnailPath":20,"statistic":1342,"gsStatistic":20,"type":162,"analyzePriority":20},[],{"issn":1329,"title":1330,"url":1331},{"VOID":13},{"EN":15},{"VOID":17},[],[],[1335],{"id":78,"indexDatabase":1336,"url":91,"indexYears":92,"academicFieldIds":1341,"indexDatabaseRanking":99},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1337,"label":1338,"description":1339,"key":88,"publicationTags":1340,"standard":20},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97,98],{"impactFactor":21,"impactFactorByYear":1343,"i10Index":112,"i10IndexLast5Year":113,"totalPublication":114,"totalPublicationByYear":1344,"totalCitation":129,"totalCitationByYear":1345,"totalCitationPerPublication":145,"totalCitationPerPublicationByYear":1346,"hindexLast5Year":161,"hindex":161},{"2012":102,"2013":103,"2014":103,"2015":104,"2016":105,"2017":106,"2018":107,"2019":108,"2020":109,"2021":104,"2022":110,"2023":111},{"2008":116,"2009":117,"2010":118,"2011":119,"2012":120,"2013":121,"2014":122,"2015":123,"2016":124,"2017":125,"2018":126,"2019":127,"2020":123,"2021":128},{"2008":131,"2009":132,"2010":133,"2011":134,"2012":135,"2013":136,"2014":137,"2015":138,"2016":139,"2017":140,"2018":141,"2019":142,"2020":143,"2021":144},{"2008":147,"2009":148,"2010":149,"2011":150,"2012":151,"2013":152,"2014":153,"2015":154,"2016":155,"2017":156,"2018":157,"2019":158,"2020":159,"2021":160},{"volume":1348,"pages":1349},{"VOID":384},{"VOID":1350},"1-13","2014-10-14",{"id":1353,"createTime":1354,"updateTime":1355,"relativeEntities":1356,"slug":1357,"properties":1358,"entityType":182,"verifyStatus":183,"verifyTime":1367,"verifyNote":184,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1368,"fullTextUrl":20,"authors":1369,"publicationType":359,"publisherRelationship":1448,"citationCount":20,"citationInfo":20,"publishDate":1474,"publishYear":727,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":389},"eb56587c-66cf-4f1e-93bf-0f35f3914a77","2024-02-19T08:16:59.634+00:00","2025-01-01T23:56:28.108+00:00",[],"Effects-of-tea-saponin-on-glucan-conversion-and-bonding-behaviour-of-cellulolytic-enzymes-during-enzymatic-hydrolysis-of-corncob-residue-with-high-lignin-content",{"references":1359,"abstract":1361,"title":1363,"doi":1365},{"VOID":1360},"Weiss N, Börjesson J, Pedersen LS, Meyer AS: Enzymatic lignocellulose hydrolysis: Improved cellulase productivity by insoluble solids recycling. Biotechnol Biofuels 2013, 6: 5. 10.1186\u002F1754-6834-6-5\nLu J, Weerasiri RR, Lee I: Carbon nanotubes tuned foam structures as novel nanostructured biocarriers for lignocellulose hydrolysis. Biotechnol Lett 2013, 35: 181-188. 10.1007\u002Fs10529-012-1066-5\nTang Y, Bu L, He J, Jiang J: L(+)-Lactic acid production from furfural residues and corn kernels with treated yeast as nutrients. Eur Food Res Technol 2013, 236: 365-371. 10.1007\u002Fs00217-012-1865-x\nLiu HQ, Feng Y, Zhao DQ, Jiang JX: Evaluation of cellulases produced from four fungi cultured on furfural residues and microcrystalline cellulose. Biodegradation 2012, 23: 465-472. 10.1007\u002Fs10532-011-9525-6\nXing Y, Bu LX, Wang K, Jiang JX: Pretreatment of furfural residues with alkaline peroxide to improve cellulose hydrolysis and characterization of isolated lignin. Cellulose Chem Technol 2012, 46: 249-260.\nLiu HQ, Feng Y, Zhao DQ, Jiang JX: Influence of cellulose content on the enzyme activity in the saccharification digests of furfural residues. Asia-Pac J Chem Eng 2012, 7: s275-s279.\nMao L, Zhang L, Gao N, Li A: FeCl 3 and acetic acid co-catalyzed hydrolysis of corncob for improving furfural production and lignin removal from residue. Bioresource Technol 2012, 123: 324-331.\nYu H, Tang Y, Xing Y, Zhu L, Jiang J: Improvement of the enzymatic hydrolysis of furfural residues by pretreatment with combined green liquor and hydrogen peroxide. Bioresource Technol 2013, 147: 29-36.\nBu L, Xing Y, Yu H, Gao Y, Jiang JX: Comparative study of sulfite pretreatments for robust enzymatic saccharification of corn cob residue. Biotechnol Biofuels 2012, 5: 87. 10.1186\u002F1754-6834-5-87\nCheng K, Wang W, Zhang J, Zhao Q, Li J, Xue J: Statistical optimization of sulfite pretreatment of corncob residues for high concentration ethanol production. Bioresource Technol 2011, 102: 3014-3019. 10.1016\u002Fj.biortech.2010.09.117\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. Bioresource Technol 2010, 101: 4952-4958. 10.1016\u002Fj.biortech.2009.11.013\nBu L, Tang Y, Gao Y, Jian H, Jiang JX: Comparative characterization of milled wood lignin from furfural residues and corncob. Chem Eng J 2011, 175: 176-184.\nXing Y, Bu LX, Zhu LW, Jiang JX: Ultrasound-assisted enzymatic hydrolysis of furfural residues after alkaline peroxide pretreatment. Chem Ind Forest Prod 2012, 32: 47-52.\nZhang L, Li T, Wang L, Li SZ: Enzymatic hydrolysis of corncob residues of furfural manufacture and optimum conditions for cellulose conversion. Trans Chin Soc Agric Eng 2009, 10: 226-230.\nSun R, Song X, Sun R, Jiang J: Effect of lignin content on enzymatic hydrolysis of furfural residues. Bioresources 2011, 6: 317-328.\nNakagame S, Chandra RP, Kadla JF: The characterization and possible role of lignin from steam and organosolv pretreated substrates on enzymatic hydrolysis [abstract]. In 32nd Symposium on Biotechnology for Fuels and Chemicals: 19–22, April, 2010. Florida; 2010:8-20.\nLee SH, Doherty TV, Linhardt RJ, Dordick JS: Ionic liquid-mediated selective extraction of lignin from wood leading to enhanced enzymatic cellulose hydrolysis. Biotechnol Bioeng 2009, 102: 1368-1376. 10.1002\u002Fbit.22179\nAlvira P, Tomás-Pejó E, Ballesteros M, Negro MJ: Pretreatment technologies for an efficient bioethanol production process based on enzymatic hydrolysis: A review. Bioresource Technol 2010, 101: 4851-4861. 10.1016\u002Fj.biortech.2009.11.093\nKumar P, Barrett DM, Delwiche MJ, Stroeve P: Methods for pretreatment of lignocellulosic biomass for efficient hydrolysis and biofuel production. Ind Eng Chem Res 2009, 48: 3713-3729. 10.1021\u002Fie801542g\nDyk JSV, Pletschke BI: A review of lignocellulose bioconversion using enzymatic hydrolysis and synergistic cooperation between enzymes-factors affecting enzymes, conversion and synergy. Biotechnol Adv 2012, 30: 1458-1480. 10.1016\u002Fj.biotechadv.2012.03.002\nZhou H, Lou H, Yang D, Zhu JY, Qiu X: Lignosulfonate to enhance enzymatic saccharification of lignocelluloses: role of molecular weight and substrate lignin. Ind Eng Chem Res 2013, 52: 8464-8470. 10.1021\u002Fie401085k\nCao S, Aita GM: Enzymatic hydrolysis and ethanol yields of combined surfactant and dilute ammonia treated sugarcane bagasse. Bioresource Technol 2013, 131: 357-364.\nEckard AD, Muthukumarappan K, Gibbons W: Enzyme recycling in a simultaneous and separate saccharification and fermentation of corn stover: A comparison between the effect of polymeric micelles of surfactants and polypeptides. Bioresource Technol 2013, 132: 202-209.\nEriksson T, Borjesson J, Tjerneld F: Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose. Enzyme Microb Technol 2002, 31: 353-364. 10.1016\u002FS0141-0229(02)00134-5\nJeya M, Kalyani D, Dhiman SS, Kim H, Woo S, Kim D, Lee J: Saccharification of woody biomass using glycoside hydrolases from Stereum hirsutum . Bioresource Technol 2012, 117: 310-316.\nYuan X, Liang Y, Zeng G, Wang W: Hydrolysis of pretreated rice straw with surfactants at low cellulase dosage. [http:\u002F\u002Fwww.paper.edu.cn\u002Freleasepaper\u002Fcontent\u002F201001-1052] []\nWang H, Fan B, Li C, Liu S, Li M: Effects of rhamnolipid on the cellulase and xylanase in hydrolysis of wheat straw. Bioresource Technol 2011, 102: 6515-6521. 10.1016\u002Fj.biortech.2011.02.102\nZhang Q, He G, Wang J, Cai W, Xu Y: Mechanisms of the stimulatory effects of rhamnolipid biosurfactant on rice straw hydrolysis. Appl Energy 2009, 86: s233-s237.\nMenon V, Prakash G, Prabhune A, Rao M: Biocatalytic approach for the utilization of hemicellulose for ethanol production from agricultural residue using thermostable xylanase and thermotolerant yeast. Bioresource Technol 2010, 101: 5366-5373. 10.1016\u002Fj.biortech.2010.01.150\nZhu XY, Lin HM, Chen X, Xie J, Wang P: Mechanochemical-assisted extraction and antioxidant activities of kaempferol glycosides from Camellia oleifera Abel. meal. J Agric Food Chem 2011, 59: 3986-3993. 10.1021\u002Fjf1042689\nJian H, Liao X, Zhu L, Zhang W, Jiang J: Synergism and foaming properties in binary mixtures of a biosurfactant derived from Camellia oleifera Abel and synthetic surfactants. J Colloid Interface Sci 2011, 359: 487-492. 10.1016\u002Fj.jcis.2011.04.038\nZhang M, Ouyang J, Liu B, Yu H, Jiang T, Cai C, Li X: Comparison of hydrolysis efficiency and enzyme adsorption of three different cellulosic materials in the presence of poly (ethylene glycol). Bioenerg Res doi:10.1007\u002Fs12155-013-9334-3\nOkino S, Ikeo M, Ueno Y, Taneda D: Effects of Tween 80 on cellulase stability under agitated conditions. Bioresource Technol 2013, 142: 535-539.\nYang M, Zhang A, Liu B, Li W, Xing J: Improvement of cellulose conversion caused by the protection of Tween-80 on the adsorbed cellulose. Biochem Eng J 2011, 56: 125-129. 10.1016\u002Fj.bej.2011.04.009\nBai Y, Lin D, Wu F, Wang Z, Xing B: Adsorption of Triton X-series surfactants and its role in stabilizing multi-walled carbon nanotube suspensions. Chemosphere 2010, 79: 362-367. 10.1016\u002Fj.chemosphere.2010.02.023\nGhose TK: Measurement of cellulaseactivities. Pure Appl Chem 1986, 59: 257-268.\nKovacs K, Szakacs G, Zacchi G: Comparative enzymatic hydrolysis of pretreated spruce by supernatants, whole fermentation broths and washed mycelia of Trichoderma reesei and Trichoderma atroviride . Bioresource Technol 2009, 100: 1350-1357. 10.1016\u002Fj.biortech.2008.08.006\nBradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72: 248-254. 10.1016\u002F0003-2697(76)90527-3",{"EN":1362},"Recently, interest in the utilization of corncob residue (CCR, with high lignin of 45.1%) as a feedstock for bioethanol has been growing. Surfactants have been one of the most popular additives intended to prevent the inhibitory effect of lignin on cellulolytic enzymes, thereby improving hydrolysis. In this study, the effects of biosurfactant tea saponin (TS) on the enzymatic hydrolysis of CCR and the bonding behavior of cellulolytic enzymes to the substrate were investigated. The surface tension in the supernatant was also detected to obtain information about the characteristics and stability of TS. The glucose concentration was 17.15 mg\u002FmL at 120 hours of hydrolysis with the low loading of cellulolytic enzymes (7.0 FPU\u002Fg cellulose and 10.5 BGU\u002Fg cellulose) and 5% CCR. The optimal dosage of TS was its critical micelle concentration (cmc, 1.80 mg\u002FmL). The glucose yield was enhanced from 34.29 to 46.28 g\u002F100 g dry matter by TS. The results indicate that TS can promote the adsorption of cellulolytic enzymes on the substrate and mediate the release of adsorbed enzymes. Meanwhile, TS improves the recovery of the cellulolytic enzymes after a hydrolysis cycle and prevents deactivation of the enzymes during the intense shaking process. The surface tension in supernatants of digested CCR with TS remained at 50.00 mN\u002Fm during the course of hydrolysis. It is interesting to note that biosurfactant TS can maintain the surface tension in supernatants, despite its digestibility by cellulolytic enzymes. Serving as an accelerant of lignocellulose hydrolysis, TS can also be degraded by the cellulolytic enzymes and release glucose while retaining stability, which reduces the cost of both the cellulolytic enzymes and the additive. As the glucose from the TS could be utilized by yeast, further efforts will investigate the mechanism of function and the application of TS in the production of ethanol by simultaneous saccharification and fermentation (SSF).",{"EN":1364},"Effects of tea saponin on glucan conversion and bonding behaviour of cellulolytic enzymes during enzymatic hydrolysis of corncob residue with high lignin 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CA, Quintero JA, Paz IC. Production of bioethanol from sugarcane bagasse: status and perspectives. Bioresour Technol. 2010;101(13):4754–66.\nKatsimpouras C, Kalogiannis KG, Kalogianni A, Lappas AA, Topakas E. Production of high concentrated cellulosic ethanol by acetone\u002Fwater oxidized pretreated beech wood. Biotechnol Biofuels. 2017;10:54.\nYousuf A. Biodiesel from lignocellulosic biomass—prospects and challenges. Waste Manag. 2012;32(11):2061–7.\nAl-Naji M, Schlaad H, Antonietti M. New (and Old) monomers from biorefineries to make polymer chemistry more sustainable. Macromol Rapid Commun. 2021;42(3):e2000485.\nDedes G, Karnaouri A, Topakas E. Novel routes in transformation of lignocellulosic biomass to furan platform chemicals: from pretreatment to enzyme catalysis. Catalysts. 2020;10(7):743.\nYuan H, Liu H, Du J, Liu K, Wang T, Liu L. Biocatalytic production of 2,5-furandicarboxylic acid: recent advances and future perspectives. Appl Microbiol Biotechnol. 2020;104(2):527–43.\nZhao P, Zhang Y, Wang Y, Cui H, Song F, Xhang L. Conversion of glucose into 5-hydroxymethylfurfural catalyzed by acid–base bifunctional heteropolyacid-based ionic hybrids. Green Chem. 2018;20:1551–9.\nJia HY, Zong MH, Zheng GW, Li N. One-pot enzyme cascade for controlled synthesis of furancarboxylic acids from 5-hydroxymethylfurfural by H2O2 internal recycling. Chemsuschem. 2019;12(21):4764–8.\nKarich A, Kleeberg SB, Ullrich R, Hofrichter M. Enzymatic preparation of 2,5-furandicarboxylic acid (FDCA)-a substitute of terephthalic acid-by the joined action of three fungal enzymes. Microorganisms. 2018;6(1):5.\nSimeonov SP, Coelho JA, Afonso CA. Integrated chemo-enzymatic production of 5-hydroxymethylfurfural from glucose. Chemsuschem. 2013;6(6):997–1000.\nHuang R, Qi W, Su R, He Z. Integrating enzymatic and acid catalysis to convert glucose into 5-hydroxymethylfurfural. Chem Commun. 2010;46(7):1115–7.\nTakasaki Y. Studies on sugar-isomerizing enzymes: effect of borate on glucose–fructose isomerization catalyzed by glucose isomerase. Agr Biol Chem. 1971;35(9):1371–5.\nWrigstedt P, Keskivali J, Repo T. Microwave-enhanced aqueous biphasic dehydration of carbohydrates to 5-hydroxymethylfurfural. RSC Adv. 2016;6:18973–9.\nRomán-Leshkov Y, Dumesic JA. Solvent effects on fructose dehydration to 5-hydroxymethylfurfural in biphasic systems saturated with inorganic salts. Top Catal. 2009;52:297–303.\nSievers C, Musin I, Marzialetti T, Olarte MBV, Agrawal PK, Jones CW. Acid-catalyzed conversion of sugars and furfurals in an ionic-liquid phase. Chemsuschem. 2009;2:665–71.\nBinder JB, Raines RT. Simple chemical transformation of lignocellulosic biomass into furans for fuels and chemicals. J Am Chem Soc. 2009;131:1979–85.\nBicker M, Kaiser D, Ott L, Vogel H. Dehydration of D-fructose to hydroxymethylfurfural in sub-and supercritical fluids. J Supercrit Fluid. 2005;36:118.\nWang W, Mittal A, Pilath H, Chen X, Tucker MP, Johnson DK. Simultaneous upgrading of biomass-derived sugars to HMF\u002Ffurfural via enzymatically isomerized ketose intermediates. Biotechnol Biofuels. 2019;12:253.\nKalogiannis G, Karnaouri A, Michailof C, Tzika AM, Asimakopoulou G, Topakas E, Lappas AA. OxiOrganosolv: a novel acid free oxidative organosolv fractionation for lignocellulose fine sugar streams. Bioresour Technol. 2020;313:123599.\nKarnaouri A, Asimakopoulou G, Kalogiannis KG, Lappas A, Topakas E. Efficient D-lactic acid production by Lactobacillus delbrueckii subsp. bulgaricus through conversion of organosolv pretreated lignocellulosic biomass. Biomass Bioenergy. 2020;140:105672.\nKarnaouri A, Chalima A, Kalogiannis KG, Varamogianni-Mamatsi D, Lappas A, Topakas E. Utilization of lignocellulosic biomass towards the production of omega-3 fatty acids by the heterotrophic marine microalga Crypthecodinium cohnii. Bioresour Technol. 2020;303:122899.\nPortillo Perez G, Agneev Mukherjee A, Dumont M-J. Insights into HMF catalysis. J Ind Eng Chem. 2019;70:1–34.\nvan Putten RJ, van der Waal JC, de Jong E, Rasrendra CB, Heeres HJ, de Vries JG. Hydroxymethylfurfural, a versatile platform chemical made from renewable resources. Chem Rev. 2013;113(3):1499–597.\nAgarwal B, Kailasam K, Sangwan RS, Elumalai S. Traversing the history of solid catalysts for heterogeneous synthesis of 5-hydroxymethylfurfural from carbohydrate sugars: a review. Renew Sust Energy Rev. 2018;82:2408–25.\nDelidovich I, Palkovits R. Catalytic isomerization of biomass-derived aldoses: a review. Chemsuschem. 2016;9:547–61.\nChoudhary V, Pinar AB, Lobo RF, Vlachos DG, Sandler SI. Comparison of homogeneous and heterogeneous catalysts for glucose-to-fructose isomerization in aqueous media. Chemsuschem. 2013;6:2369–76.\nLi H, Yang S, Saravanamurugan S, Riisager A. Glucose isomerization by enzymes and chemo-catalysts: status and current advances. ACS Catal. 2017;7:3010–29.\nSzijártó N, Horan E, Zhang J, Puranen T, Siika-Aho M, Viikari L. Thermostable endoglucanases in the liquefaction of hydrothermally pretreated wheat straw. Biotechnol Biofuels. 2011;4(1):2.\nMarianou AA, Michailof CM, Pineda A, Iliopoulou EF, Triantafyllidis KS, Lappas AA. Effect of Lewis and Brønsted acidity on glucose conversion to 5-HMF and lactic acid in aqueous and organic media. Appl Catal A Gen. 2018;555:75–87.\nStåhlberg T, Rodriguez-Rodriguez S, Fristrup P, Riisager A. Metal-free dehydration of glucose to 5-(hydroxymethyl)furfural in ionic liquids with boric acid as a promoter. Chem Eur J. 2011;17:1456–64.\nIstasse T, Lemaur V, Debroux G, Bockstal L, Lazzaroni R, Richel A. Monosaccharides dehydration assisted by formation of borate esters of α-hydroxyacids in choline chloride-based low melting mixtures. Front Chem. 2020;8:569.\nXu Z-L, Wang X-Y, Shen M-Y, Du C-H. Synthesis of 5-hydroxymethylfurfural from glucose in a biphasic medium with AlCl3 and boric acid as the catalyst. Chem Pap. 2016;12:1649–57.\nZhao Y, Lu K, Xu H, Zhu L, Wang S. A critical review of recent advances in the production of furfural and 5-hydroxymethylfurfural from lignocellulosic biomass through homogeneous catalytic hydrothermal conversion. Renew Sustain Energy Rev. 2021;139:110706.\nAkien GR, LHorváth QiIT. Molecular mapping of the acid catalysed dehydration of fructose. Chem Commun. 2012;48:5850–2.\nRivas S, Vila C, Alonso JL, Santos V, Parajó JC, Leahy JJ. Biorefinery processes for the valorization of Miscanthus polysaccharides: from constituent sugars to platform chemicals. Ind Crops Prod. 2019;134:309–17.\nHansen TS, Mielby J, Riisager A. Synergy of boric acid and added salts in the catalytic dehydration of hexoses to 5-hydroxymethylfurfural in water. Green Chem. 2011;13:109–14.\nBaugh KD, McCarty PL. Thermochemical pretreatment of lignocellulose to enhance methane fermentation: I. Monosaccharide and furfurals hydrothermal decomposition and product formation rates. Biotechnol Bioeng. 1988;31(1):50–61.\nSluiter JB, Ruiz RO, Scarlata CJ, Sluiter AD, Templeton DW. Compositional analysis of lignocellulosic feedstocks. 1. Review and description of methods. J Agric Food Chem. 2010;58:9043–53.\nBradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Anal Biochem. 1976;72:248–54.\nGhose T. Measurement of cellulase activities. Pure Appl Chem. 2009;59(2):257–68.\nMiller GL. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem. 1959;31:426–8.\nKarnaouri AC, Topakas E, Christakopoulos P. Cloning, expression, and characterization of a thermostable GH7 endoglucanase from Myceliophthora thermophila capable of high-consistency enzymatic liquefaction. Appl Microbiol Biotechnol. 2014;98(1):231–42.",{"EN":1485},"Over the last few years, valorization of lignocellulosic biomass has been expanded beyond the production of second-generation biofuels to the synthesis of numerous platform chemicals to be used instead of their fossil-based counterparts. One such well-researched example is 5-hydroxymethylfurfural (HMF), which is preferably produced by the dehydration of fructose. Fructose is obtained by the isomerization of glucose, which in turn is derived by the hydrolysis of cellulose. However, to avoid harsh reaction conditions with high environmental impact, an isomerization step towards fructose is necessary, as fructose can be directly dehydrated to HMF under mild conditions. This work presents an optimized process to produce fructose from beechwood biomass hydrolysate and subsequently convert it to HMF by employing homogeneous catalysis. The optimal saccharification conditions were identified at 10% wt. solids loading and 15 mg enzyme\u002Fgsolids, as determined from preliminary trials on pure cellulose (Avicel® PH-101). Furthermore, since high rate glucose isomerization to fructose requires the addition of sodium tetraborate, the optimum borate to glucose molar ratio was determined to 0.28 and was used in all experiments. Among 20 beechwood solid pulps obtained from different organosolv pretreatment conditions tested, the highest fructose production was obtained with acetone (160 °C, 120 min), reaching 56.8 g\u002F100 g pretreated biomass. A scale-up hydrolysis in high solids (25% wt.) was then conducted. The hydrolysate was subjected to isomerization eventually leading to a high-fructose solution (104.5 g\u002FL). Dehydration of fructose to HMF was tested with 5 different catalysts (HCl, H3PO4, formic acid, maleic acid and H-mordenite). Formic acid was found to be the best one displaying 79.9% sugars conversion with an HMF yield and selectivity of 44.6% and 55.8%, respectively. Overall, this work shows the feasibility of coupling bio- and chemo-catalytic processes to produce HMF from lignocellulose in an environmentally friendly manner. Further work for the deployment of biocatalysts for the oxidation of HMF to its derivatives could pave the way for the emergence of an integrated process to effectively produce biobased monomers from lignocellulose.",{"EN":1487},"Conversion of organosolv pretreated hardwood biomass into 5-hydroxymethylfurfural (HMF) by combining enzymatic hydrolysis and isomerization with homogeneous catalysis",{"VOID":1489},"10.1186\u002Fs13068-021-02022-9","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13068-021-02022-9",[1492,1507,1534,1546,1558,1570,1589],{"id":1493,"sortIndex":206,"researcher":20,"roles":1494,"affiliations":1495,"properties":1504},"b629357a-cb3a-4f06-9fbb-bb7f6f3fc23d",[191],[1496],{"id":20,"sortIndex":21,"affiliation":1497,"properties":20},{"id":1498,"createTime":1499,"updateTime":1499,"relativeEntities":1500,"slug":20,"properties":1501,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"7d338147-d203-435f-a524-4a1dc146f9fd","2024-02-06T02:35:12.172+00:00",[],{"title":1502},{"VI":1503},"Center for Research and Technology Hellas, Chemical Process and Energy Resources Institute, Thessaloniki, Greece",{"title":1505},{"VI":1506},"Chrysoula M. Michailof",{"id":1508,"sortIndex":219,"researcher":20,"roles":1509,"affiliations":1510,"properties":1531},"6c946af1-0334-4ce2-b970-fa1ebc96f1cf",[191],[1511,1519],{"id":20,"sortIndex":21,"affiliation":1512,"properties":20},{"id":1513,"createTime":1514,"updateTime":1514,"relativeEntities":1515,"slug":20,"properties":1516,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"afa9428b-7161-47a8-a33c-a0ac3e74ea5b","2024-02-06T02:35:12.358+00:00",[],{"title":1517},{"VI":1518},"Industrial Biotechnology & Biocatalysis Group, School of Chemical Engineering, National Technical University of Athens, Zografou Campus, Athens, Greece",{"id":1520,"sortIndex":219,"affiliation":1521,"properties":1530},"9022a4b4-fc14-45da-88fb-c66bcb742c67",{"id":1522,"createTime":1523,"updateTime":1524,"relativeEntities":1525,"slug":1526,"properties":1527,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"5474fa3a-9b28-40a8-a1b7-031d139eb742","2023-12-08T10:20:04.496+00:00","2024-09-21T08:39:11.875+00:00",[],"Biochemical-Process-Engineering-Chemical-Engineering-Department-of-Civil-Environmental-and-Natural-Resources-Engineering-Lule%C3%A5-University-of-Technology-Lule%C3%A5-Sweden",{"title":1528},{"VI":1529},"Biochemical Process Engineering, Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, Sweden",{},{"title":1532},{"VI":1533},"Anthi Karnaouri",{"id":1535,"sortIndex":21,"researcher":20,"roles":1536,"affiliations":1537,"properties":1543},"e6442bb1-2f2b-4db8-b937-3d94cc67b432",[191],[1538],{"id":20,"sortIndex":21,"affiliation":1539,"properties":20},{"id":1513,"createTime":1514,"updateTime":1514,"relativeEntities":1540,"slug":20,"properties":1541,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1542},{"VI":1518},{"title":1544},{"VI":1545},"Grigorios Dedes",{"id":1547,"sortIndex":189,"researcher":20,"roles":1548,"affiliations":1549,"properties":1555},"e5742b04-8c25-4d79-863f-3b244912918b",[191],[1550],{"id":20,"sortIndex":21,"affiliation":1551,"properties":20},{"id":1498,"createTime":1499,"updateTime":1499,"relativeEntities":1552,"slug":20,"properties":1553,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1554},{"VI":1503},{"title":1556},{"VI":1557},"Konstantinos G. Kalogiannis",{"id":1559,"sortIndex":340,"researcher":20,"roles":1560,"affiliations":1561,"properties":1567},"7e6f08a9-cf06-4524-a254-56471d3d0837",[191],[1562],{"id":20,"sortIndex":21,"affiliation":1563,"properties":20},{"id":1498,"createTime":1499,"updateTime":1499,"relativeEntities":1564,"slug":20,"properties":1565,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1566},{"VI":1503},{"title":1568},{"VI":1569},"Angelos A. Lappas",{"id":1571,"sortIndex":253,"researcher":20,"roles":1572,"affiliations":1573,"properties":1586},"6309aee2-997d-44dc-a68b-638510699a2e",[191],[1574,1581],{"id":1575,"sortIndex":219,"affiliation":1576,"properties":1580},"690773f2-2940-4a7c-845a-8a80d1388d50",{"id":1522,"createTime":1523,"updateTime":1524,"relativeEntities":1577,"slug":1526,"properties":1578,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1579},{"VI":1529},{},{"id":20,"sortIndex":21,"affiliation":1582,"properties":20},{"id":1513,"createTime":1514,"updateTime":1514,"relativeEntities":1583,"slug":20,"properties":1584,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1585},{"VI":1518},{"title":1587},{"VI":1588},"Evangelos Topakas",{"id":1590,"sortIndex":281,"researcher":20,"roles":1591,"affiliations":1592,"properties":1598},"285477e0-2b65-4f71-a7da-57f7fc8d8172",[191],[1593],{"id":20,"sortIndex":21,"affiliation":1594,"properties":20},{"id":1498,"createTime":1499,"updateTime":1499,"relativeEntities":1595,"slug":20,"properties":1596,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1597},{"VI":1503},{"title":1599},{"VI":1600},"Asimina A. Marianou",{"url":1490,"publisher":1602,"properties":1623},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1603,"slug":10,"properties":1604,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1608,"manageAffiliations":1609,"indexDatabases":1610,"url":20,"thumbnailPath":20,"statistic":1618,"gsStatistic":20,"type":162,"analyzePriority":20},[],{"issn":1605,"title":1606,"url":1607},{"VOID":13},{"EN":15},{"VOID":17},[],[],[1611],{"id":78,"indexDatabase":1612,"url":91,"indexYears":92,"academicFieldIds":1617,"indexDatabaseRanking":99},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1613,"label":1614,"description":1615,"key":88,"publicationTags":1616,"standard":20},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97,98],{"impactFactor":21,"impactFactorByYear":1619,"i10Index":112,"i10IndexLast5Year":113,"totalPublication":114,"totalPublicationByYear":1620,"totalCitation":129,"totalCitationByYear":1621,"totalCitationPerPublication":145,"totalCitationPerPublicationByYear":1622,"hindexLast5Year":161,"hindex":161},{"2012":102,"2013":103,"2014":103,"2015":104,"2016":105,"2017":106,"2018":107,"2019":108,"2020":109,"2021":104,"2022":110,"2023":111},{"2008":116,"2009":117,"2010":118,"2011":119,"2012":120,"2013":121,"2014":122,"2015":123,"2016":124,"2017":125,"2018":126,"2019":127,"2020":123,"2021":128},{"2008":131,"2009":132,"2010":133,"2011":134,"2012":135,"2013":136,"2014":137,"2015":138,"2016":139,"2017":140,"2018":141,"2019":142,"2020":143,"2021":144},{"2008":147,"2009":148,"2010":149,"2011":150,"2012":151,"2013":152,"2014":153,"2015":154,"2016":155,"2017":156,"2018":157,"2019":158,"2020":159,"2021":160},{"volume":1624,"pages":1626},{"VOID":1625},"14",{"VOID":386},"2021-08-28",2021,{"id":1630,"createTime":1631,"updateTime":1631,"relativeEntities":1632,"slug":20,"properties":1633,"entityType":182,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1642,"fullTextUrl":20,"authors":1643,"publicationType":359,"publisherRelationship":1743,"citationCount":20,"citationInfo":20,"publishDate":1770,"publishYear":1771,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":389},"63c9b0d7-fd6e-4125-beea-bc84e80a8fec","2024-01-16T23:55:56.616+00:00",[],{"references":1634,"abstract":1636,"title":1638,"doi":1640},{"VOID":1635},"Robak K, Balcerek M. Review of second generation bioethanol production from residual biomass. Food Technol Biotechnol. 2018;56:174–87.\nLee J. Biological conversion of lignocellulosic biomass to ethanol. J Biotechnol. 1997;56:1–24.\nHendriks ATWM, Zeeman G. Pretreatments to enhance the digestibility of lignocellulosic biomass. Bioresour Technol. 2009;100:10–8.\nHou J, Qiu C, Shen Y, Li H, Bao X. Engineering of Saccharomyces cerevisiae for the efficient co-utilization of glucose and xylose. FEMS Yeast Res. 2017;17:fox034.\nJeppsson M, Bengtsson O, Franke K, Lee H, Hahn-Hägerdal B, Gorwa-Grauslund MF. The expression of a Pichia stipitis xylose reductase mutant with higher K m for NADPH increases ethanol production from xylose in recombinant Saccharomyces cerevisiae. Biotechnol Bioeng. 2006;93:665–73.\nWatanabe S, Saleh AA, Pack SP, Annaluru N, Kodaki T, Makino K. Ethanol production from xylose by recombinant Saccharomyces cerevisiae expressing protein engineered NADP+-dependent xylitol dehydrogenase. J Biotechnol. 2007;130:316–9.\nKarhumaa K, Fromanger R, Hahn-Hägerdal B, Gorwa-Grauslund MF. High activity of xylose reductase and xylitol dehydrogenase improves xylose fermentation by recombinant Saccharomyces cerevisiae. Appl Microbiol Biotechnol. 2007;73:1039–46.\nMatsushika A, Sawayama S. Efficient bioethanol production from xylose by recombinant Saccharomyces cerevisiae requires high activity of xylose reductase and moderate xylulokinase activity. J Biosci Bioeng. 2008;106:306–9.\nZeng WY, Tang YQ, Gou M, Sun ZY, Xia ZY, Kida K. Comparative transcriptomes reveal novel evolutionary strategies adopted by Saccharomyces cerevisiae with improved xylose utilization capability. Appl Microbiol Biotechnol. 2017;101:1753–67.\nSarthy AV, McConaughy BL, Lobo Z, Sundstrom JA, Furlong CE, Hall BD. Expression of the Escherichia coli xylose isomerase gene in Saccharomyces cerevisiae. Appl Environ Microbiol. 1987;53:1996–2000.\nAmore R, Wilhelm M, Hollenberg CP. The fermentation of xylose—an analysis of the expression of Bacillus and Actinoplanes xylose isomerase genes in yeast. Appl Microbiol Biotechnol. 1989;30:351–7.\nMoes CJ, Pretorius IS, van Zyl WH. Cloning and expression of the Clostridium thermosulfurogenes d-xylose isomerase gene (xylA) in Saccharomyces cerevisiae. Biotechnol Lett. 1996;18:269–74.\nWalfridsson M, Bao X, Anderlund M, Lilius G, Bülow L, Hahn-Hägerdal B. Ethanolic fermentation of xylose with Saccharomyces cerevisiae harboring the Thermus thermophilus xylA gene, which expresses an active xylose (glucose) isomerase. Appl Environ Microbiol. 1996;62:4648–51.\nKuyper M, Harhangi HR, Stave AK, Winkler AA, Jetten MS, de Laat WT, den Ridder JJ, Op den Camp HJ, van Dijken JP, Pronk JT. High-level functional expression of a fungal xylose isomerase: the key to efficient ethanolic fermentation of xylose by Saccharomyces cerevisiae? FEMS Yeast Res. 2003;4:69–78.\nMadhavan A, Tamalampudi S, Srivastava A, Fukuda H, Bisaria VS, Kondo A. Alcoholic fermentation of xylose and mixed sugars using recombinant Saccharomyces cerevisiae engineered for xylose utilization. Appl Microbiol Biotechnol. 2009;82:1037–47.\nMadhavan A, Tamalampudi S, Ushida K, Kanai D, Katahira S, Srivastava A, Fukuda H, Bisaria VS, Kondo A. Xylose isomerase from polycentric fungus Orpinomyces: gene sequencing, cloning, and expression in Saccharomyces cerevisiae for bioconversion of xylose to ethanol. Appl Microbiol Biotechnol. 2009;82:1067–78.\nTanino T, Hotta A, Ito T, Ishii J, Yamada R, Hasunuma T, Ogino C, Ohmura N, Ohshima T, Kondo A. Construction of a xylose-metabolizing yeast by genome integration of xylose isomerase gene and investigation of the effect of xylitol on fermentation. Appl Microbiol Biotechnol. 2010;88:1215–21.\nBrat D, Boles E, Wiedemann B. Functional expression of a bacterial xylose isomerase in Saccharomyces cerevisiae. Appl Environ Microbiol. 2009;75:2304–11.\nDemeke MM, Dietz H, Li Y, Foulquié-Moreno MR, Mutturi S, Deprez S, Den Abt T, Bonini BM, Liden G, Dumortier F, Verplaetse A, Boles E, Thevelein JM. Development of a d-xylose fermenting and inhibitor tolerant industrial Saccharomyces cerevisiae strain with high performance in lignocellulose hydrolysates using metabolic and evolutionary engineering. Biotechnol Biofuels. 2013;6:89.\nAeling KA, Salmon KA, Laplaza JM, Li L, Headman JR, Hutagalung AH, Picataggio S. Co-fermentation of xylose and cellobiose by an engineered Saccharomyces cerevisiae. J Ind Microbiol Biotechnol. 2012;39:1597–604.\nHector RE, Dien BS, Cotta MA, Mertens JA. Growth and fermentation of d-xylose by Saccharomyces cerevisiae expressing a novel d-xylose isomerase originating from the bacterium Prevotella ruminicola TC2-24. Biotechnol Biofuels. 2013;6:84.\nde Figueiredo Vilela L, de Mello VM, Reis VC, Bon EP, Gonçalves Torres FA, Neves BC, Eleutherio EC. Functional expression of Burkholderia cenocepacia xylose isomerase in yeast increases ethanol production from a glucose–xylose blend. Bioresour Technol. 2013;128:792–6.\nde Figueiredo Vilela L, de Araujo VPG, de Sousa Paredes R, da Silva Bon EP, Torres FAG, Neves BC, Eleutherio ECA. Enhanced xylose fermentation and ethanol production by engineered Saccharomyces cerevisiae strain. AMB Express. 2015;5:1–7.\nHarcus D, Dignard D, Lépine G, Askew C, Raymond M, Whiteway M, Wu C. Comparative xylose metabolism among the ascomycetes C. albicans, S. stipitis and S. cerevisiae. PLoS ONE. 2013;8:e80733.\nWaltman MJ, Yang ZK, Langan P, Graham DE, Kovalevsky A. Engineering acidic Streptomyces rubiginosus d-xylose isomerase by rational enzyme design. Protein Eng Des Sel. 2014;27:59–64.\nLee SM, Jellison T, Alper HS. Directed evolution of xylose isomerase for improved xylose catabolism and fermentation in the yeast Saccharomyces cerevisiae. Appl Environ Microbiol. 2012;78:5708–16.\nHarhangi HR, Akhmanova AS, Emmens R, van der Drift C, de Laat WT, van Dijken JP, Jetten MS, Pronk JT, Op den Camp HJ. Xylose metabolism in the anaerobic fungus Piromyces sp. strain E2 follows the bacterial pathway. Arch Microbiol. 2003;180:134–41.\nVan Maris AJ, Winkler AA, Kuyper M, De Laat WT, Van Dijken JP, Pronk JT. Development of efficient xylose fermentation in Saccharomyces cerevisiae: xylose isomerase as a key component. Adv Biochem Eng Biotechnol. 2007;108:179–204.\nXia PF, Zhang GC, Liu JJ, Kwak S, Tsai CS, Kong II, Sung BH, Sohn JH, Wang SG, Jin YS. GroE chaperonins assisted functional expression of bacterial enzymes in Saccharomyces cerevisiae. Biotechnol Bioeng. 2016;113:2149–55.\nTemer B, Dos Santos LV, Negri VA, Galhardo JP, Magalhães PHM, José J, Marschalk C, Corrêa TLR, Carazzolle MF, Pereira GAG. Conversion of an inactive xylose isomerase into a functional enzyme by co-expression of GroEL-GroES chaperonins in Saccharomyces cerevisiae. BMC Biotechnol. 2017;17:71.\nZhang GC, Liu JJ, Kong II, Kwak S, Jin YS. Combining C6 and C5 sugar metabolism for enhancing microbial bioconversion. Curr Opin Chem Biol. 2015;29:49–57.\nMoysés DN, Reis VC, de Almeida JR, de Moraes LM, Torres FA. Xylose Fermentation by Saccharomyces cerevisiae: challenges and prospects. Int J Mol Sci. 2016;17:207.\nRose M. Molecular and biochemical characterization of the hexokinase from the starch-utilizing yeast Schwanniomyces occidentalis. Curr Genet. 1995;27:330–8.\nDemeke MM, Foulquié-Moreno MR, Dumortier F, Thevelein JM. Rapid evolution of recombinant Saccharomyces cerevisiae for xylose fermentation through formation of extra-chromosomal circular DNA. PLoS Genet. 2015;11:e1005010.\nBoles E, Schulte F, Miosga T, Freidel K, Schlüter E, Zimmermann FK, Hollenberg CP, Heinisch JJ. Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate. J Bacteriol. 1997;179:2987–93.\nKobayashi Y, Sahara T, Suzuki T, Kamachi S, Matsushika A, Hoshino T, Ohgiya S, Kamagata Y, Fujimori KE. Genetic improvement of xylose metabolism by enhancing the expression of pentose phosphate pathway genes in Saccharomyces cerevisiae IR-2 for high-temperature ethanol production. J Ind Microbiol Biotechnol. 2017;44:879–91.\nKobayashi Y, Sahara T, Ohgiya S, Kamagata Y, Fujimori KE. Systematic optimization of gene expression of pentose phosphate pathway enhances ethanol production from a glucose\u002Fxylose mixed medium in a recombinant Saccharomyces cerevisiae. AMB Express. 2018;8:139.\nSedlak M, Ho NW. Characterization of the effectiveness of hexose transporters for transporting xylose during glucose and xylose co-fermentation by a recombinant Saccharomyces yeast. Yeast. 2004;21:671–84.\nFarwick A, Bruder S, Schadeweg V, Oreb M, Boles E. Engineering of yeast hexose transporters to transport d-xylose without inhibition by d-glucose. Proc Natl Acad Sci USA. 2014;111:5159–64.\nLi YC, Mitsumasu K, Gou ZX, Gou M, Tang YQ, Li GY, Wu XL, Akamatsu T, Taguchi H, Kida K. Xylose fermentation efficiency and inhibitor tolerance of the recombinant industrial Saccharomyces cerevisiae strain NAPX37. Appl Microbiol Biotechnol. 2016;100:1531–42.\nKuriyama H, Seiko Y, Murakami T, Kobayashi H. Continuous ethanol fermentation with cell recycling using flocculating yeast. J Ferment Technol. 1985;63:159–65.\nSahara T, Fujimori KE, Nezuo M, Tsukahara M, Tochigi Y, Ohgiya S, Kamagata Y. Draft genome sequence of Saccharomyces cerevisiae IR-2, a useful industrial strain for highly efficient production of bioethanol. Genome Announc. 2014;2:e01160-13.\nGüldener U, Heck S, Fielder T, Beinhauer J, Hegemann JH. A new efficient gene disruption cassette for repeated use in budding yeast. Nucleic Acids Res. 1996;24:2519–24.\nAkashi H. Translational selection and yeast proteome evolution. Genetics. 2003;164:1291–303.\nOhgiya S, Sahara T. Protein production at low temperature by yeast Saccharomyces cerevisiae. Biosci Ind. 2007;65:130–1.\nMatsushika A, Watanabe S, Kodaki T, Makino K, Inoue H, Murakami K, Takimura O, Sawayama S. Expression of protein engineered NADP+-dependent xylitol dehydrogenase increase ethanol production from xylose in recombinant Saccharomyces cerevisiae. Appl Microbiol Biotechnol. 2008;81:243–55.",{"EN":1637},"Expression of d-xylose isomerase having high catalytic activity in Saccharomyces cerevisiae (S. cerevisiae) is a prerequisite for efficient and economical production of bioethanol from cellulosic biomass. Although previous studies demonstrated functional expression of several xylose isomerases (XI) in S. cerevisiae, identification of XIs having higher catalytic activity is needed. Here, we report a new strategy to improve xylose fermentation in the S. cerevisiae strain IR-2 that involves an evolutionary engineering to select top-performing XIs from eight previously reported XIs derived from various species. Eight XI genes shown to have good expression in S. cerevisiae were introduced into the strain IR-2 having a deletion of GRE3 and XKS1 overexpression that allows use of d-xylose as a carbon source. Each transformant was evaluated under aerobic and micro-aerobic culture conditions. The strain expressing XI from Lachnoclostridium phytofermentans ISDg (LpXI) had the highest d-xylose consumption rate after 72 h of micro-aerobic fermentation on d-glucose and d-xylose mixed medium. To enhance LpXI catalytic activity, we performed random mutagenesis using error-prone polymerase chain reaction (PCR), which yielded two LpXI candidates, SS82 and SS92, that showed markedly improved fermentation performance. The LpXI genes in these clones carried either T63I or V162A\u002FN303T point mutations. The SS120 strain expressing LpXI with the double mutation of T63I\u002FV162A assimilated nearly 85 g\u002FL d-glucose and 35 g\u002FL d-xylose to produce 53.3 g\u002FL ethanol in 72 h with an ethanol yield of approximately 0.44 (g\u002Fg-input sugars). An in vitro enzyme assay showed that, compared to wild-type, the LpXI double mutant in SS120 had a considerably higher Vmax (0.107 µmol\u002Fmg protein\u002Fmin) and lower Km (37.1 mM). This study demonstrated that LpXI has the highest d-xylose consumption rate among the XIs expressed in IR-2 under micro-aerobic co-fermentation conditions. A combination of novel mutations (T63I and V162A) significantly improved the enzymatic activity of LpXI, indicating that LpXI-T63I\u002FV162A would be a potential construct for highly efficient production of cellulosic ethanol.",{"EN":1639},"Molecular evolutionary engineering of xylose isomerase to improve its catalytic activity and performance of micro-aerobic glucose\u002Fxylose co-fermentation in Saccharomyces cerevisiae",{"VOID":1641},"10.1186\u002Fs13068-019-1474-z","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13068-019-1474-z",[1644,1659,1674,1696,1719,1731],{"id":1645,"sortIndex":206,"researcher":20,"roles":1646,"affiliations":1647,"properties":1656},"d233b36a-e8a8-441e-a284-d333b74ff9b4",[191],[1648],{"id":20,"sortIndex":21,"affiliation":1649,"properties":20},{"id":1650,"createTime":1651,"updateTime":1651,"relativeEntities":1652,"slug":20,"properties":1653,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"a15cd6f7-142d-4994-8bbc-a83a03decbb6","2024-02-14T14:04:04.204+00:00",[],{"title":1654},{"VI":1655},"Bioproduction Research Institute (BPRI), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan",{"title":1657},{"VI":1658},"Yoichi Kamagata",{"id":1660,"sortIndex":189,"researcher":20,"roles":1661,"affiliations":1662,"properties":1671},"c66879c4-bc45-42e3-ae4c-662a5b94eb77",[191],[1663],{"id":20,"sortIndex":21,"affiliation":1664,"properties":20},{"id":1665,"createTime":1666,"updateTime":1666,"relativeEntities":1667,"slug":20,"properties":1668,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"88b85eec-da35-4354-af88-2dd0c8120237","2024-01-16T23:55:56.683+00:00",[],{"title":1669},{"VI":1670},"Bioproduction Research Institute (BPRI), National Institute of Advanced Industrial Science and Technology (AIST), Sapporo, Japan",{"title":1672},{"VI":1673},"Satoru Ohgiya",{"id":1675,"sortIndex":219,"researcher":20,"roles":1676,"affiliations":1677,"properties":1693},"7cdb22a2-355b-40f5-8b16-2c49742e0eea",[191],[1678,1683],{"id":20,"sortIndex":21,"affiliation":1679,"properties":20},{"id":1650,"createTime":1651,"updateTime":1651,"relativeEntities":1680,"slug":20,"properties":1681,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1682},{"VI":1655},{"id":1684,"sortIndex":219,"affiliation":1685,"properties":1692},"4a4470d9-7003-45c9-a9a4-b60113ca3e0a",{"id":1686,"createTime":1687,"updateTime":1687,"relativeEntities":1688,"slug":20,"properties":1689,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"86465165-c5ae-4807-9853-1d3afed7cc19","2024-01-16T23:55:56.657+00:00",[],{"title":1690},{"VI":1691},"Biomaterial in Tokyo Company Limited, Kashiwa, Japan",{},{"title":1694},{"VI":1695},"Yosuke Kobayashi",{"id":1697,"sortIndex":21,"researcher":20,"roles":1698,"affiliations":1699,"properties":1716},"a71a638f-31b7-40c2-a140-8ca5d7cf48d3",[191],[1700,1711],{"id":1701,"sortIndex":219,"affiliation":1702,"properties":1710},"29413039-417d-4d42-936a-a373c3a8b1e5",{"id":1703,"createTime":1704,"updateTime":1704,"relativeEntities":1705,"slug":1706,"properties":1707,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"5037640e-68aa-45ff-ad08-98a4a30d7998","2024-04-11T10:11:44.804+00:00",[],"Center-for-Biosystems-Dynamics-Research-BDR-RIKEN-Suita-Japan",{"title":1708},{"EN":1709},"Center for Biosystems Dynamics Research (BDR), RIKEN, Suita, Japan",{},{"id":20,"sortIndex":21,"affiliation":1712,"properties":20},{"id":1650,"createTime":1651,"updateTime":1651,"relativeEntities":1713,"slug":20,"properties":1714,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1715},{"VI":1655},{"title":1717},{"VI":1718},"Taisuke Seike",{"id":1720,"sortIndex":340,"researcher":20,"roles":1721,"affiliations":1722,"properties":1728},"25d05bf5-dafe-47cd-8108-b196b78799ab",[191],[1723],{"id":20,"sortIndex":21,"affiliation":1724,"properties":20},{"id":1650,"createTime":1651,"updateTime":1651,"relativeEntities":1725,"slug":20,"properties":1726,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1727},{"VI":1655},{"title":1729},{"VI":1730},"Kazuhiro E. Fujimori",{"id":1732,"sortIndex":281,"researcher":20,"roles":1733,"affiliations":1734,"properties":1740},"9a0725cf-4320-4a58-9a4e-ee1f6408c0ac",[191],[1735],{"id":20,"sortIndex":21,"affiliation":1736,"properties":20},{"id":1650,"createTime":1651,"updateTime":1651,"relativeEntities":1737,"slug":20,"properties":1738,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1739},{"VI":1655},{"title":1741},{"VI":1742},"Takehiko Sahara",{"url":1642,"publisher":1744,"properties":1765},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1745,"slug":10,"properties":1746,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1750,"manageAffiliations":1751,"indexDatabases":1752,"url":20,"thumbnailPath":20,"statistic":1760,"gsStatistic":20,"type":162,"analyzePriority":20},[],{"issn":1747,"title":1748,"url":1749},{"VOID":13},{"EN":15},{"VOID":17},[],[],[1753],{"id":78,"indexDatabase":1754,"url":91,"indexYears":92,"academicFieldIds":1759,"indexDatabaseRanking":99},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1755,"label":1756,"description":1757,"key":88,"publicationTags":1758,"standard":20},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97,98],{"impactFactor":21,"impactFactorByYear":1761,"i10Index":112,"i10IndexLast5Year":113,"totalPublication":114,"totalPublicationByYear":1762,"totalCitation":129,"totalCitationByYear":1763,"totalCitationPerPublication":145,"totalCitationPerPublicationByYear":1764,"hindexLast5Year":161,"hindex":161},{"2012":102,"2013":103,"2014":103,"2015":104,"2016":105,"2017":106,"2018":107,"2019":108,"2020":109,"2021":104,"2022":110,"2023":111},{"2008":116,"2009":117,"2010":118,"2011":119,"2012":120,"2013":121,"2014":122,"2015":123,"2016":124,"2017":125,"2018":126,"2019":127,"2020":123,"2021":128},{"2008":131,"2009":132,"2010":133,"2011":134,"2012":135,"2013":136,"2014":137,"2015":138,"2016":139,"2017":140,"2018":141,"2019":142,"2020":143,"2021":144},{"2008":147,"2009":148,"2010":149,"2011":150,"2012":151,"2013":152,"2014":153,"2015":154,"2016":155,"2017":156,"2018":157,"2019":158,"2020":159,"2021":160},{"volume":1766,"pages":1768},{"VOID":1767},"12",{"VOID":1769},"1-16","2019-06-06",2019,{"id":1773,"createTime":1774,"updateTime":1775,"relativeEntities":1776,"slug":1777,"properties":1778,"entityType":182,"verifyStatus":183,"verifyTime":1775,"verifyNote":184,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":219,"primaryUrl":1787,"fullTextUrl":20,"authors":1788,"publicationType":359,"publisherRelationship":1898,"citationCount":20,"citationInfo":20,"publishDate":1924,"publishYear":1925,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":389},"5f61c3f4-a097-4f52-b2dc-590860c3f0d8","2024-01-15T11:08:19.886+00:00","2025-02-22T23:55:54.070+00:00",[],"Engineering-vesicle-trafficking-improves-the-extracellular-activity-and-surface-display-efficiency-of-cellulases-in-Saccharomyces-cerevisiae",{"references":1779,"abstract":1781,"title":1783,"doi":1785},{"VOID":1780},"Cabezón T, De WM, Herion P, Loriau R, Bollen A. 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Curr Opin Biotechnol. 2005;16:577–83.\nMatano Y, Hasunuma T, Kondo A. Display of cellulases on the cell surface of Saccharomyces cerevisiae for high yield ethanol production from high-solid lignocellulosic biomass. BioresourTechnol. 2012;108:128–33.\nLambertz C, Garvey M, Klinger J, Heesel D, Klose H, Fischer R, Commandeur U. Challenges and advances in the heterologous expression of cellulolytic enzymes: a review. Biotechnol Biofuels. 2014;7:135.\nCai H, Reinisch K, Ferro-Novick S. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell. 2007;12:671–82.\nGrosshans BL, Ortiz D, Novick P. Rabs and their effectors achieving specificity in membrane traffic. Proc Natl Acad Sci USA. 2006;103:11821–7.\nWhyte JR, Munro S. Vesicle tethering complexes in membrane traffic. J Cell Sci. 2002;115:2627–37.\nJahn R, Scheller RH. SNAREs—engines for membrane fusion. Nat Rev Mol Cell Biol. 2006;7:631–43.\nMalsam J, Kreye S, Söllner T. Membrane traffic in the secretory pathway: membrane fusion: SNAREs and regulation. Cell Mol Life Sci. 2008;65:2814–32.\nGrote E, Vlacich G, Pypaert M, Novick PJ. A snc1 endocytosis mutant: phenotypic analysis and suppression by overproduction of dihydrosphingosine phosphate lyase. Mol Biol Cell. 2000;11:4051–65.\nAalto M, Ronne H, Keränen S. Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. EMBO J. 1993;12:4095.\nSchÖNholzer F, Schweingruber A-M, Trachsel H, Schweingruber ME. Intracellular maturation and secretion of acid phosphatase of Saccharomyces cerevisiae. Eur J Biochem. 1985;147:273–9.\nRuohonen L, Toikkanen J, Outola M, Soderlund H, Keranen S. Enhancement of protein secretion in Saccharomyces cerevisiae by overproduction of Sso protein, a late-acting component of the secretory machinery. Yeast. 1997;13:337–51.\nXu L, Shen Y, Hou J, Peng B, Tang H, Bao X. Secretory pathway engineering enhances secretion of cellobiohydrolase I from Trichoderma reesei in Saccharomyces cerevisiae. J Biosci Bioeng. 2014;117:45–52.\nWeber-Boyvat M. Functional role of the Mso1p-Sec1p complex in membrane fusion regulation. J Colloid Interf Sci. 1988;122(2):336–45.\nZhang X, Wang P, Gangar A, Zhang J, Brennwald P, TerBush D, Guo W. Lethal giant larvae proteins interact with the exocyst complex and are involved in polarized exocytosis. J Cell Biol. 2005;170:273–83.\nHou J, Tyo KEJ, Liu Z, Petranovic D, Nielsen J. Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae. FEMS Yeast Res. 2012;12(5):491–510.\nHou J, Tyo K, Liu Z, Petranovic D, Nielsen J. Engineering of vesicle trafficking improves heterologous protein secretion in Saccharomyces cerevisiae. Metab Eng. 2012;14:120–7.\nToikkanen JH, Miller KJ, Söderlund H, Jäntti J, Keränen S. The β subunit of the Sec61p Endoplasmic Reticulum translocon interacts with the exocyst complex in Saccharomyces cerevisiae. J Biol Chem. 2003;278:20946–53.\nKondo A, Ueda M. Yeast cell-surface display—applications of molecular display. Appl Microbiol Biotechnol. 2004;64:28–40.\nWen F, Sun J, Zhao H. Yeast surface display of trifunctional minicellulosomes for simultaneous saccharification and fermentation of cellulose to ethanol. Appl Microbiol Biotechnol. 2010;76(4):1251–60.\nInokuma K, Hasunuma T, Kondo A. Efficient yeast cell-surface display of exo- and endo-cellulase using the SED1 anchoring region and its original promoter. Biotechnol Biofuels. 2014;7(1):965–9.\nVaart JMVD, Biesebeke RT, Chapman JW, Toschka HY, Klis FM, Verrips CT. Comparison of cell wall proteins of Saccharomyces cerevisiae as anchors for cell surface expression of heterologous proteins. Appl Microbiol Biotechnol. 1997;63(2):615–20.\nMatsuoka H, Hashimoto K, Saijo A, Takada Y, Kondo A, Ueda M, Ooshima H, Tachibana T, Azuma M. Cell wall structure suitable for surface display of proteins in Saccharomyces cerevisiae. Yeast. 2014;31(2):67–76.\nKuroda K, Matsui K, Higuchi S, Sahara H, Hata Y. Enhancement of display efficiency in yeast display system by vector engineering and gene disruption. Appl Microbiol Biotechnol. 2009;82(4):713–9.\nd’Enfert C, Wuestehube LJ, Lila T, Schekman R. Sec12p-dependent membrane binding of the small GTP-binding protein Sar1p promotes formation of transport vesicles from the ER. J Cell Biol. 1991;114:663–70.\nČopič A, Latham CF, Horlbeck MA, D’Arcangelo JG, Miller EA. ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p. Science. 2012;335:1359–62.\nMuñiz M, Nuoffer C, Hauri H-P, Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum—derived vesicles. 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Optimization of amino acid supplements for heterologous protein secretion in Saccharomyces cerevisiae. Biotechnol Tech. 1994;8:161–6.\nGibson DG. Enzymatic assembly of overlapping DNA fragments. Methods Enzymol. 2011;498:349–61.\nPeng B, Yu S, Li X, Xiao C, Jin H, Bao X. Improvement of xylose fermentation in respiratory-deficient xylose-fermenting Saccharomyces cerevisiae. Metab Eng. 2012;14:9–18.\nTang H, Bao X, Shen Y, Song M, Wang S, Wang C, Hou J. Engineering protein folding and translocation improves heterologous protein secretion in Saccharomyces cerevisiae. Biotechnol Bioeng. 2015;112:1872–82.\nWang C, Shen Y, Zhang Y, Suo F, Hou J, Bao X. Improvement of L-arabinose fermentation by modifying the metabolic pathway and transport in Saccharomyces cerevisiae. Biomed Res Int. 2013;2013:461204.\nBerghem LE, Pettersson LG. The mechanism of enzymatic cellulose degradation. Isolation and some properties of a beta-glucosidase from Trichoderma viride. Eur J Biochem. 1974;46:295–305.\nHasunuma T, Kondo A. Development of yeast cell factories for consolidated bioprocessing of lignocellulose to bioethanol through cell surface engineering. Biotechnol Adv. 2012;30:1207–18.\nTang HT, Shen Y, Yang H, Bao X. High β-glucosidase secretion in Saccharomyces cerevisiae improves the efficiency of cellulase hydrolysis and ethanol production in simultaneous saccharification and fermentation. J Microbiol Biotechnol. 2013;23:1576–84.\nDen Haan R, Rose SH, Lynd LR, van Zyl WH. Hydrolysis and fermentation of amorphous cellulose by recombinant Saccharomyces cerevisiae. Metab Eng. 2007;9:87–94.\nLambertz C, Garvey M, Klinger J, Heesel D, Klose H, Fischer R, Commandeur U. Challenges and advances in the heterologous expression of cellulolytic enzymes: a review. Biotechnol Biofuels. 2013;7:1–15.\nTanaka T, Yamada R, Ogino C, Kondo A. Recent developments in yeast cell surface display toward extended applications in biotechnology. Appl Microbiol Biotechnol. 2012;95:577–91.\nVan Zyl J, Den Haan R, Van Zyl W. Over-expression of native Saccharomyces cerevisiae exocytic SNARE genes increased heterologous cellulase secretion. Appl Microbiol Biotechnol. 2014;98:5567–78.\nBiemans R, Thines D, Rutgers T, De WM, Cabezon T. The large surface protein of hepatitis B virus is retained in the yeast endoplasmic reticulum and provokes its unique enlargement. DNA Cell Biol. 1991;10(3):191–200.\nSmith JD, Tang BC, Robinson AS. Protein disulfide isomerase, but not binding protein, overexpression enhances secretion of a non-disulfide-bonded protein in yeast. Biotechnol Bioeng. 2004;85(3):340–50.\nYeasmin S, Kim CH, Park HJ, Sheikh MI, Ji YL, Kim JW, Back KK, Kim SH. Cell surface display of cellulase activity-free xylanase enzyme on Saccharomyces cerevisiae EBY100. Appl Biochem Biotechnol. 2011;164:294–304.\nFan LH, Tan TW. Self-surface assembly of cellulosomes with two miniscaffoldins on Saccharomyces cerevisiae for cellulosic ethanol production. Proc Natl Acad Sci USA. 2012;109:13260–5.\nSpringer S, Chen E, Duden R, Marzioch M, Rowley A, Hamamoto S, Merchant S, Schekman R. The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae. Proc Natl Acad Sci USA. 2000;97(8):4034–9.\nCastillon GA, Aguileraromero A, Manzanolopez J, Epstein S, Kajiwara K, Funato K, Watanabe R, Riezman H, Muñiz M. The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling. Mol Biol Cell. 2011;22(16):2924–36.\nBelden WJ, Barlowe C. Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport. J Biol Chem. 1996;271(43):26939–46.\nGurunathan S, David D, Gerst JE. Dynamin and clathrin are required for the biogenesis of a distinct class of secretory vesicles in yeast. EMBO J. 2002;21(4):602–14.\nHarsay BE, Bretscher A. Parallel secretory pathways to the cell surface in yeast. J Cell Biol. 1995;131(2):297–310.\nInokuma K, Bamba T, Ishii J, Ito Y, Hasunuma T, Kondo A. Enhanced cell-surface display and secretory production of cellulolytic enzymes with Saccharomyces cerevisiae Sed1 signal peptide. Biotechnol Bioeng. 2016;113(11):2358–66.\nBreinig F, Schmitt MJ. Spacer-elongated cell wall fusion proteins improve cell surface expression in the yeast Saccharomyces cerevisiae. Appl Microbiol Biotechnol. 2002;58(5):637–44.\nIdiris A, Tohda H, Kumagai H, Takegawa K. Engineering of protein secretion in yeast: strategies and impact on protein production. Appl Microbiol Biotechnol. 2010;86(2):403–17.",{"EN":1782},"Cellulase expression via extracellular secretion or surface display in Saccharomyces cerevisiae is one of the most frequently used strategies for a consolidated bioprocess (CBP) of cellulosic ethanol production. However, the inefficiency of the yeast secretory pathway often results in low production of heterologous proteins, which largely limits cellulase secretion or display. In this study, the components of the vesicle trafficking from the endoplasmic reticulum (ER) to the Golgi and from the Golgi to the plasma membrane, involved in vesicle budding, tethering and fusion, were over-expressed in Clostridium thermocellum endoglucanase (CelA)- and Sacchromycopsis fibuligera β-glucosidase (BGL1)-secreting or -displaying strains. Engineering the targeted components in the ER to Golgi vesicle trafficking, including Sec12p, Sec13p, Erv25p and Bos1p, enhanced the extracellular activity of CelA. However, only Sec13p over-expression increased BGL1 secretion. By contrast, over-expression of the components in the Golgi to plasma membrane vesicle trafficking, including Sso1p, Snc2p, Sec1p, Exo70p, Ypt32p and Sec4p, showed better performance in increasing BGL1 secretion compared to CelA secretion, and the over-expression of these components all increased BGL1 extracellular activity. These results revealed that various cellulases showed different limitations in protein transport, and engineering vesicle trafficking has protein-specific effects. Importantly, we found that engineering the above vesicle trafficking components, particularly from the ER to the Golgi, also improved the display efficiency of CelA and BGL1 when a-agglutinin was used as surface display system. Further analyses illustrated that the display efficiency of a-agglutinin was increased by engineering vesicle trafficking, and the trend was consistent with displayed CelA and BGL1. These results indicated that fusion with a-agglutinin may affect the proteins’ properties and alter the rate-limiting step in the vesicle trafficking. We have demonstrated, for the first time, engineering vesicle trafficking from the ER to the Golgi and from the Golgi to the plasma membrane can enhance the protein display efficiency. We also found that different heterologous proteins had specific limitations in vesicle trafficking pathway and that engineering the vesicle trafficking resulted in a protein-specific effect. These results provide a new strategy to improve the extracellular secretion and surface display of cellulases in S. cerevisiae.",{"EN":1784},"Engineering vesicle trafficking improves the extracellular activity and surface display efficiency of cellulases in Saccharomyces cerevisiae",{"VOID":1786},"10.1186\u002Fs13068-017-0738-8","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13068-017-0738-8",[1789,1804,1816,1828,1840,1852,1874,1886],{"id":1790,"sortIndex":21,"researcher":20,"roles":1791,"affiliations":1792,"properties":1801},"f97758f5-1aaf-4992-96c4-a032f3819042",[191],[1793],{"id":20,"sortIndex":21,"affiliation":1794,"properties":20},{"id":1795,"createTime":1796,"updateTime":1796,"relativeEntities":1797,"slug":20,"properties":1798,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"1dd39e4b-8dcb-4516-84ef-46d729a8a21b","2024-01-15T11:08:19.930+00:00",[],{"title":1799},{"VI":1800},"The School of Life Science, State Key Laboratory of Microbial Technology, Shandong University, Jinan, China",{"title":1802},{"VI":1803},"Hongting 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Accessed 11 Apr 2020.\nMarkewitz D. Fossil fuel carbon emissions from silviculture: impacts on net carbon sequestration in forests. Forest Ecol Manag. 2006;236:153–61.\nAmateis RL, Liu J, Ducey MJ, Lee AH. Modeling response to midrotation nitrogen and phosphorus fertilization in loblolly pine plantations. South J Appl Forestry. 2000;24:207–12.\nVerschuyl J, Riffell S, Miller D, Wigley TB. Biodiversity response to intensive biomass production from forest thinning in North American forests—a meta-analysis. Forest Ecol Manag. 2011;261:221–32.\nDickens ED, Moorhead DJ. A guide to thinning pine plantations. University of Georgia; 2015. https:\u002F\u002Fbugwoodcloud.org\u002Fbugwood\u002Fproductivity\u002Fpdfs\u002FGuide_thinning_pine_plantations.pdf. Accessed 19 May 2020.\nNebeker TE, Hodges JD, Karr BK, Moehring DM. Thinning practices in southern pines-with pest management recommendations. USDA Forest Service; 1985. http:\u002F\u002Fageconsearch.umn.edu\u002Fbitstream\u002F156818\u002F2\u002Ftb1703.pdf. Accessed 19 May 2019.\nMann WF, Lohrey RE. Precommercial thinning of southern pines. J Forest. 1974;72:557–60.\nBlakeslee GM, Jokela EJ, Hollis CH, Wilson DS, Lante WD, Allen JE. Pitch canker in young loblolly pines: influence of precommercial thinning and fertilization on disease incidence and severity. South J Appl Forestry. 1999;23:139–43.\nWatson AC, Sullivan J, Amacher GS, Asaro C. Cost sharing for pre-commercial thinning in southern pine plantations: willingness to participate in Virginia’s pine bark beetle prevention program. Forest Policy Econ. 2013;34:65–72.\nEdmunds CW, Reyes Molina EA, André N, Hamilton C, Park S, Fasina O, et al. Blended feedstocks for thermochemical conversion: biomass characterization and bio-oil production from switchgrass-pine residues blends. Front Energy Res. 2018;6:79.\nGallagher TV, Kantavichai R, Teeter LD. An economic analysis of incorporating biomass thinning into loblolly pine plantations in Alabama. Open J Forestry. 2017;7:172–87.\nMederski P, Venanzi R, Bembenek M, Karaszewski Z, Rosińska M, Pilarek Z, et al. Designing thinning operations in 2nd age class pine stands—economic and environmental implications. Forests. 2018;9:335.\nJenkins JC, Chojnacky DC, Heath LS, Birdsey RA. National-scale biomass estimators for united states tree species. Forest Sci. 2003;49:12–35.\nLangholtz MH, Stokes BJ, Eaton LM. 2016 Billion-ton report: advancing domestic resources for a thriving bioeconomy, vol 1: economic availability of feedstocks. Oak Ridge National Laboratory, Oak Ridge, TN, USA; 2016. https:\u002F\u002Fwww.energy.gov\u002Fsites\u002Fprod\u002Ffiles\u002F2016\u002F12\u002Ff34\u002F2016_billion_ton_report_12.2.16.pdf. Accessed 18 May 2020.\nFritts SR, Moorman CE, Hazel DW, Jackson BD. Biomass Harvesting Guidelines affect downed woody debris retention. Biomass Bioenerg. 2014;70:382–91.\nLan K, Kelley SS, Nepal P, Yao Y. Dynamic life cycle carbon and energy analysis for cross-laminated timber in the Southeastern United States. Environ Res Lett. 2020;15(12):124036.\nWang M, Han J, Dunn JB, Cai H. Well-to-wheels energy use and greenhouse gas emissions of ethanol from corn, sugarcane and cellulosic biomass for US use. Environ Res Lett. 2012;7:045905.\nDaystar J, Reeb C, Gonzalez R, Venditti R, Kelley SS. Environmental life cycle impacts of cellulosic ethanol in the Southern U.S. produced from loblolly pine, eucalyptus, unmanaged hardwoods, forest residues, and switchgrass using a thermochemical conversion pathway. Fuel Processing Technol. 2015;138:164–74.\nISO. ISO 14041: 1998 Environmental management — Life cycle assessment—goal and scope definition and inventory analysis; 1998. https:\u002F\u002Fwww.iso.org\u002Fstandard\u002F23152.html. Accessed 11 Apr 2020.\nDwivedi P, Alavalapati JR, Susaeta A, Stainback A. Impact of carbon value on the profitability of slash pine plantations in the southern United States: an integrated life cycle and Faustmann analysis. Can J Forest Res. 2009;39:990–1000.\nOneil EE, Johnson LR, Lippke BR, McCarter JB, McDill ME, Roth PA, et al. Life-cycle impacts of inland Northwest and Northeast\u002FNorth central forest resources. Wood Fiber Sci. 2010;42:29–51.\nKilpeläinen A, Alam A, Strandman H, Kellomäki S. Life cycle assessment tool for estimating net CO2 exchange of forest production. GCB Bioenergy. 2011;3:461–71.\nJohnson L, Lippke B, Oneil E. Modeling biomass collection and woods processing life-cycle analysis. Forest Product J. 2012;62:258–72.\nKarjalainen T. Greenhouse gas emissions from the use of primary energy in forest operations and long-distance transportation of timber in Finland. Forestry. 1996;69:215–28.\nLindholm E. Energy Use and Environmental Impact of Roundwood and Forest Fuel Production in Sweden. Dissertation. Uppsala: Swedish University of Agricultural Sciences Energy; 2010.\nAlam A, Kilpeläinen A, Kellomäki S. Impacts of initial stand density and thinning regimes on energy wood production and management-related CO2 emissions in boreal ecosystems. Eur J Forest Res. 2012;131:655–67.\nWhittaker C, Mortimer N, Murphy R, Matthews R. Energy and greenhouse gas balance of the use of forest residues for bioenergy production in the UK. Biomass Bioenerg. 2011;35:4581–94.\nGonzález-García S, Berg S, Feijoo G, Moreira MT. Environmental impacts of forest production and supply of pulpwood: Spanish and Swedish case studies. Int J Life Cycle Assess. 2009;14:340–53.\nKarjalainen T, Kellomäki S, Pussinen A. Role of wood-based products in absorbing atmospheric carbon. Silva Fennica. 1994;28:67–80.\nKlvac R, Skoupy A. Characteristic fuel consumption and exhaust emissions in fully mechanized logging operations. J Forest Res. 2009;14:328–34.\nAthanassiadis D, Lidestav G, Wästerlund I. Fuel, hydraulic oil and lubricant consumption in Swedish mechanized harvesting operations, 1996. J Forest Eng. 1999;10:59–66.\nSaud P, Wang J, Lin W, Sharma BD, Hartley DS. A life cycle analysis of forest carbon balance and carbon emissions of timber harvesting in West Virginia. Wood Fiber Sci. 2013;45:250–67.\nMcNamee P, Adams PW, McManus MC, Dooley B, Darvell LI, Williams A, et al. An assessment of the torrefaction of North American pine and life cycle greenhouse gas emissions. Energy Convers Manag. 2016;113:177–88.\nMcEwan A, Brink M, Spinelli R. Efficiency of different machine layouts for chain flail delimbing. Debarking Chipping For. 2019;10:126.\nSchultz RP. Loblolly pine: the ecology and culture of loblolly pine (Pinus taeda L.). USDA Forest Service, Washington D.C., USA; 1997. https:\u002F\u002Fwww.srs.fs.usda.gov\u002Fpubs\u002F734. Accessed 11 Apr 2020.\nPatterson DW, Doruska PF, Posey T. Weight and bulk density of loblolly pine plywood logs in southeast Arkansas. 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University of Georgia; 2002. https:\u002F\u002Fbugwoodcloud.org\u002Fresource\u002Ffiles\u002F14828.pdf. Accessed 19 Jun 2019.\nOu L, Kim H, Kelley S, Park S. Impacts of feedstock properties on the process economics of fast-pyrolysis biorefineries. Biofuel Bioprod Bior. 2018;12:442–52.\nRinger M, Putsche V, Scahill J. Large-scale pyrolysis oil production: a technology assessment and economic analysis. National Renewable Energy Laboratory, Golden, CO, USA; 2006. https:\u002F\u002Fwww.nrel.gov\u002Fdocs\u002Ffy07osti\u002F37779.pdf. Accessed 18 Feb 2019.\nBridgwater AV, Czernik S, Piskorz J. An overview of fast pyrolysis of biomass. Org Geochem. 1999;30:1479–93.\nBridgwater AV, Peacocke GVC. Fast pyrolysis processes for biomass. Renew Sustain Energy Revs. 2000;4:1–73.\nde la Rosa JM, Rosado M, Paneque M, Miller AZ, Knicker H. Effects of aging under field conditions on biochar structure and composition: implications for biochar stability in soils. Sci Total Environ. 2018;613–614:969–76.\nMchenry MP. Agriculture, Ecosystems and Environment Agricultural bio-char production, renewable energy generation and farm carbon sequestration in Western Australia: certainty, uncertainty and risk. Agr Ecosyst Environ. 2009;129:1–7.\nLehmann J, Joseph S, editors. Biochar for environmental management: science, technology and implementation. New York: Routledge; 2015.\nIPCC. 2019 Refinement to the 2006 IPCC Guidelines for National Greenhouse Gas Inventories. Buendia EC, Tanabe K, Kranjc A, Baasansuren J, Fukuda M, Ngarize S, et al, eds. Switzerland: IPCC; 2019. https:\u002F\u002Fwww.ipcc.ch\u002Fsite\u002Fassets\u002Fuploads\u002F2019\u002F12\u002F19R_V0_01_Overview.pdf. Accessed 18 Jan 2021.\nKim S, Dale BE, Jin M, Thelen KD, Zhang X, Meier P, et al. Integration in a depot-based decentralized biorefinery system: corn stover-based cellulosic biofuel. GCB Bioenergy. 2019;11:871–82.\nWinjobi O, Zhou W, Kulas D, Nowicki J, Shonnard DR. Production of hydrocarbon fuel using two-step torrefaction and fast pyrolysis of pine. Part 2: life-cycle carbon footprint. ACS Sustain Chem Eng. 2017;5:4541–51.\nISO. ISO 14044: 2006 Environmental management—life cycle assessment—requirements and guidelines; 2006. https:\u002F\u002Fwww.iso.org\u002Fstandard\u002F38498.html. Accessed 11 Apr 2020.\nIPCC. Climate Change 2007: The physical science basis. Contribution of Working Group I to the Fourth Assessment Report of the Intergovernmental Panel on Climate Change. Solomon S, Qin D, Manning M, Chen Z, Marquis M, Averyt KB, et al., editors. Cambridge, United Kingdom and New York, NY, USA: Cambridge University Press; 2007.",{"EN":1936},"Woody biomass has been considered as a promising feedstock for biofuel production via thermochemical conversion technologies such as fast pyrolysis. Extensive Life Cycle Assessment studies have been completed to evaluate the carbon intensity of woody biomass-derived biofuels via fast pyrolysis. However, most studies assumed that woody biomass such as forest residues is a carbon–neutral feedstock like annual crops, despite a distinctive timeframe it takes to grow woody biomass. Besides, few studies have investigated the impacts of forest dynamics and the temporal effects of carbon on the overall carbon intensity of woody-derived biofuels. This study addressed such gaps by developing a life-cycle carbon analysis framework integrating dynamic modeling for forest and biorefinery systems with a time-based discounted Global Warming Potential (GWP) method developed in this work. The framework analyzed dynamic carbon and energy flows of a supply chain for biofuel production from pine residues via fast pyrolysis. The mean carbon intensity of biofuel given by Monte Carlo simulation across three pine growth cases ranges from 40.8–41.2 g CO2e MJ−1 (static method) to 51.0–65.2 g CO2e MJ−1 (using the time-based discounted GWP method) when combusting biochar for energy recovery. If biochar is utilized as soil amendment, the carbon intensity reduces to 19.0–19.7 g CO2e MJ−1 (static method) and 29.6–43.4 g CO2e MJ−1 in the time-based method. Forest growth and yields (controlled by forest management strategies) show more significant impacts on biofuel carbon intensity when the temporal effect of carbon is taken into consideration. Variation in forest operations and management (e.g., energy consumption of thinning and harvesting), on the other hand, has little impact on the biofuel carbon intensity. The carbon temporal effect, particularly the time lag of carbon sequestration during pine growth, has direct impacts on the carbon intensity of biofuels produced from pine residues from a stand-level pine growth and management point of view. The carbon implications are also significantly impacted by the assumptions of biochar end-of-life cases and forest management strategies.",{"EN":1938},"Dynamic life-cycle carbon analysis for fast pyrolysis biofuel produced from pine residues: implications of carbon temporal effects",{"VOID":1940},"10.1186\u002Fs13068-021-02027-4","https:\u002F\u002Fbiotechnologyforbiofuels.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13068-021-02027-4",[1943,1958,1984,1996,2008,2020,2037,2049],{"id":1944,"sortIndex":253,"researcher":20,"roles":1945,"affiliations":1946,"properties":1955},"a6383e2c-e941-4d0c-8746-bda508d6a4f9",[191],[1947],{"id":20,"sortIndex":21,"affiliation":1948,"properties":20},{"id":1949,"createTime":1950,"updateTime":1950,"relativeEntities":1951,"slug":20,"properties":1952,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"34441485-2b55-40b7-b896-c6ba11438ffc","2024-01-12T20:12:51.750+00:00",[],{"title":1953},{"VI":1954},"Systems Assessment Center, Energy Systems Division, Argonne National Laboratory, Lemont, USA",{"title":1956},{"VI":1957},"Hao Cai",{"id":1959,"sortIndex":269,"researcher":20,"roles":1960,"affiliations":1961,"properties":1981},"222fadca-b011-4331-91cc-b77d9ca511f2",[191],[1962,1971],{"id":20,"sortIndex":21,"affiliation":1963,"properties":20},{"id":1964,"createTime":1965,"updateTime":1965,"relativeEntities":1966,"slug":1967,"properties":1968,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"b34060d1-47db-41e6-b68c-658de74b36c3","2024-04-19T09:00:59.853+00:00",[],"Department-of-Forest-Biomaterials-North-Carolina-State-University-Raleigh-USA",{"title":1969},{"EN":1970},"Department of Forest Biomaterials, North Carolina State University, Raleigh, USA",{"id":1972,"sortIndex":219,"affiliation":1973,"properties":1980},"6567320a-ff6d-47a1-b9b1-99d02b4234ba",{"id":1974,"createTime":1975,"updateTime":1975,"relativeEntities":1976,"slug":20,"properties":1977,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"5b9ae534-08e0-4c94-a92b-40e04172595d","2024-01-12T20:12:51.784+00:00",[],{"title":1978},{"VI":1979},"Center for Industrial Ecology, Yale School of the Environment, Yale University, New Haven, USA",{},{"title":1982},{"VI":1983},"Yuan Yao",{"id":1985,"sortIndex":219,"researcher":20,"roles":1986,"affiliations":1987,"properties":1993},"2ff1cc89-8664-489a-b320-bcc8ec0810bf",[191],[1988],{"id":20,"sortIndex":21,"affiliation":1989,"properties":20},{"id":1949,"createTime":1950,"updateTime":1950,"relativeEntities":1990,"slug":20,"properties":1991,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1992},{"VI":1954},{"title":1994},{"VI":1995},"Longwen Ou",{"id":1997,"sortIndex":281,"researcher":20,"roles":1998,"affiliations":1999,"properties":2005},"e5f9736c-5b9f-4c78-bbdf-a7560f75d927",[191],[2000],{"id":20,"sortIndex":21,"affiliation":2001,"properties":20},{"id":1964,"createTime":1965,"updateTime":1965,"relativeEntities":2002,"slug":1967,"properties":2003,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":2004},{"EN":1970},{"title":2006},{"VI":2007},"Sunkyu Park",{"id":2009,"sortIndex":189,"researcher":20,"roles":2010,"affiliations":2011,"properties":2017},"3d3b7436-8a87-430e-b900-eacf0c7534d4",[191],[2012],{"id":20,"sortIndex":21,"affiliation":2013,"properties":20},{"id":1964,"createTime":1965,"updateTime":1965,"relativeEntities":2014,"slug":1967,"properties":2015,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":2016},{"EN":1970},{"title":2018},{"VI":2019},"Stephen S. 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