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In the present study, DNJ production by Bacillus subtilis subsp. inaquosorum KCTC 13429 (B. subtilis IWT) was confirmed and a mutant B. subtilis I.247 strain showing 52% increased DNJ production than wild-type strain after cultivation in 5% defatted soybean meal (DFS) for five days was isolated by UV random mutagenesis. The optimum culture conditions to maximize DNJ production by B. subtilis I.247 was predicted using response surface methodology to cultivate in medium containing 3.4% sorbitol and 2.4% yeast extract as carbon and nitrogen sources, respectively, at a temperature of 32°C. Under these conditions B. subtilis I.247 was able to produce 359 mg\u002FL after five days of cultivation. Furthermore, when the B. subtilis I.247 transformant harboring a vector expressing a gabT1-yktc1-gutB1 DNJ biosynthetic gene cluster was cultured under the optimized condition, DNJ production was increased to 773 mg\u002FL, representing a level 6.2-fold higher than that of the wild-type strain cultured in 5% DFS for five days.",{"EN":212,"VI":213},"Enhanced Production of 1-Deoxynojirimycin in Bacillus subtilis subsp. inaquosorum by Random Mutagenesis and Culture Optimization","Tăng cường sản xuất 1-Deoxynojirimycin ở Bacillus subtilis subsp. inaquosorum bằng đột biến ngẫu nhiên và tối ưu hóa điều kiện nuôi cấy",{"VOID":215},"Gao, K., C. Zheng, T. Wang, H. Zhao, J. Wang, Z. Wang, X. Zhai, Z. Jia, J. Chen, Y. Zhou, and W. Wang (2016) 1-Deoxynojirimycin: occurrence, extraction, chemistry, oral pharmacokinetics, biological activities and in silico target fishing. Molecules. 21: 1600.\nZhang, W., W. Mu, H. Wu, and Z. Liang (2019) An overview of the biological production of 1-deoxynojirimycin: current status and future perspective. Appl. Microbiol. Biotechnol. 103: 9335–9344.\nWatson, A. A., G. W. Fleet, N. Asano, R. J. Molyneux, and R. J. Nash (2001) Polyhydroxylated alkaloids — natural occurrence and therapeutic applications. Phytochemistry. 56: 265–295.\nDwek, R. A., T. D. Butters, F. M. Platt, and N. Zitzmann (2002) Targeting glycosylation as a therapeutic approach. Nat. Rev. Drug Discov. 1: 65–75.\nKiefel, M. J. (2010) Glycomimetics as inhibitors in anti-infection therapy. pp. 915–932. In: O. Holst, P. J. Brennan, and M. von Itzstein (eds.). Microbial Glycobiology. Elsevier, San Diego, CA, USA.\nLi, Y., S. Zhong, J. Yu, Y. Sun, J. Zhu, D. Ji, and C. Wu (2019) The mulberry-derived 1-deoxynojirimycin (DNJ) inhibits high-fat diet (HFD)-induced hypercholesteremia and modulates the gut microbiota in a gender-specific manner. J. Funct. Foods. 52: 63–72.\nZheng, J., L. Zhu, B. Hu, X. Zou, H. Hu, Z. Zhang, N. Jiang, J. Ma, H. Yang, and H. Liu (2019) 1-Deoxynojirimycin improves high fat diet-induced nonalcoholic steatohepatitis by restoring gut dysbiosis. J. Nutr. Biochem. 71: 16–26.\nAfarinkia, K. and A. Bahar (2005) Recent advances in the chemistry of azapyranose sugars. Tetrahedron Asymmetry. 16: 1239–1287.\nHardick, D. J., D. W. Hutchinson, S. J. Trew, and E. M. Wellington (1992) Glucose is a precursor of 1-deoxynojirimycin and 1-deoxymannonojirimycin in Streptomyces subrutilus. Tetrahedron. 48: 6285–6296.\nHardick, D. J. and D. W. Hutchinson (1993) The biosynthesis of 1-deoxynojirimycin in Bacillus subtilis var niger. Tetrahedron. 49: 6707–6716.\nClark, L. F., J. V. Johnson, and N. A. Horenstein (2011) Identification of a gene cluster that initiates azasugar biosynthesis in Bacillus amyloliquefaciens. Chembiochem. 12: 2147–2150.\nKang, K. D., Y. S. Cho, J. H. Song, Y. S. Park, J. Y. Lee, K. Y. Hwang, S. K. Rhee, J. H. Chung, O. Kwon, and S. I. Seong (2011) Identification of the genes involved in 1-deoxynojirimycin synthesis in Bacillus subtilis MORI 3K-85. J. Microbiol. 49: 431–440.\nStein, D. C., L. K. Kopec, R. E. Yasbin, and F. E. Young (1984) Characterization of Bacillus subtilis DSM704 and its production of 1-deoxynojirimycin. Appl. Environ. Microbiol. 48: 280–284.\nSchedel, M. (2001) Regioselective oxidation of aminosorbitol with Gluconobacter oxydans, key reaction in the industrial 1-deoxynojirimycin synthesis. pp. 295–311. In: H. J. Rehm and G. Reed (eds.). Biotechnology Set. Wiley-VCH, Weinheim, Germany.\nWei, Z. J., L. C. Zhou, H. Chen, and G. H. Chen (2011) Optimization of the fermentation conditions for 1-deoxynojirimycin production by Streptomyces lawendulae applying the response surface methodology. Int. J. Food Eng. 7: 16.\nEzure, Y., S. Maruo, K. Miyazaki, and M. Kawamata (1985) Moranoline (1-deoxynojirimycin) fermentation and its improvement. Agric. Biol. Chem. 49: 1119–1125.\nZhu, Y. P., X. T. Li, C. Teng, and B. G. Sun (2013) Enhanced production of α-glucosidase inhibitor by a newly isolated strain of Bacillus subtilis B2 using response surface methodology. Food Bioprod. Process. 91: 264–270.\nCho, Y. S., Y. S. Park, J. Y. Lee, K. D. Kang, K. Y. Hwang, and S. I. Seong (2008) Hypoglycemic effect of culture broth of Bacillus subtilis S10 producing 1-deoxynojirimycin. J. Korean Soc. Food Sci. Nutr. 37: 1401–1407.\nLee, H., H. H. Shin, H. R. Kim, Y. D. Nam, D. H. Seo, and M. J. Seo (2018) Culture optimization strategy for 1-deoxynojirimycin-producing Bacillus methylotrophicus K26 isolated from Korean fermented soybean paste, Doenjang. Biotechnol. Bioprocess Eng. 23: 424–431.\nWu, H., Y. Guo, L. Chen, G. Chen, and Z. Liang (2019) A novel strategy to regulate 1-deoxynojirimycin production based on its biosynthetic pathway in Streptomyces lavendulae. Front. Microbiol. 10: 1968.\nWu, Y., J. Arciola, and N. Horenstein (2014) Medium-chain dehydrogenases with new specificity: amino mannitol dehydrogenases on the azasugar biosynthetic pathway. Protein Pept. Lett. 21: 10–14.\nArciola, J. M. and N. A. Horenstein (2018) Characterization of the PLP-dependent transaminase initiating azasugar biosynthesis. Biochem. J. 475: 2241–2256.\nJiang, P., S. Mu, H. Li, Y. Li, C. Feng, J. M. Jin, and S. Y. Tang (2015) Design and application of a novel high-throughput screening technique for 1-deoxynojirimycin. Sci Rep. 5: 8563.\nRayamajhi, V., D. Dhakal, A. K. Chaudhary, and J. K. Sohng (2018) Improved production of 1-deoxynojirymicin in Escherichia coli through metabolic engineering. World J. Microbiol. Biotechnol. 34: 77.\nNijland, R., J. G. Burgess, J. Errington, and J. W. Veening (2010) Transformation of environmental Bacillus subtilis isolates by transiently inducing genetic competence. PLoS One. 5: e9724.\nGu, Y., X. Xu, Y. Wu, T. Niu, Y. Liu, J. Li, G. Du, and L. Liu (2018) Advances and prospects of Bacillus subtilis cellular factories: From rational design to industrial applications. Metab. Eng. 50: 109–121.\nJeong, D. E., Y. So, S. Y. Park, S. H. Park, and S. K. Choi (2018) Random knock-in expression system for high yield production of heterologous protein in Bacillus subtilis. J. Biotechnol. 266: 50–58.\nLim, H. and S. K. Choi (2019) Programmed gRNA removal system for CRISPR-Cas9-mediated multi-round genome editing in Bacillus subtilis. Front. Microbiol. 10: 1140.\nSambrook, J. and D. W. Russell (2001) Molecular Cloning: A Laboratory Manual. 3rd ed., pp. 116–119. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA.\nTransformation of Bacillus subtilis (simple). http:\u002F\u002F2014.igem.org\u002Fwiki\u002Fimages\u002Fc\u002Fc2\u002FLMU_Munich14_Transformation_of_Bacillus_subtilis.pdf.\nLe Breton, Y., N. P. Mohapatra, and W. G. Haldenwang (2006) In vivo random mutagenesis of Bacillus subtilis by use of TnYLB-1, a mariner-based transposon. Appl. Environ. Microbiol. 72: 327–333.\nAltenbuchner, J. (2016) Editing of the Bacillus subtilis genome by the CRISPR-Cas9 system. Appl. Environ. Microbiol. 82: 5421–5427.\nNguyen, H. D., T. T. P. Phan, and W. Schumann (2007) Expression vectors for the rapid purification of recombinant proteins in Bacillus subtilis. Curr. Microbiol. 55: 89–93.\nGopinath, K. P., S. Murugesan, J. Abraham, and K. Muthukumar (2009) Bacillus sp. mutant for improved biodegradation of Congo red: random mutagenesis approach. Bioresour. Technol. 100: 6295–6300.\nKotlar, C. E., M. V. Agüero, and S. I. Roura (2010) Methods: Simultaneous optimization of biomass and protease biosynthesis by a local isolated Pseudomonas sp. — response surface optimization using Box-Behnken design. Ind. Biotechnol. 6: 364–374.\nRairakhwada, D., J. W. Seo, M. Y. Seo, O. Kwon, S. K. Rhee, and C. H. Kim (2010) Gene cloning, characterization, and heterologous expression of levansucrase from Bacillus amyloliquefaciens. J. Ind. Microbiol. Biotechnol. 37: 195–204.\nKim, J. W., S. U. Kim, H. S. Lee, I. Kim, M. Y. Ahn, and K. S. Ryu (2003) Determination of 1-deoxynojirimycin in Morus alba L. leaves by derivatization with 9-fluorenylmethyl chloroformate followed by reversed-phase high-performance liquid chromatography. J. Chromatogr. A. 1002: 93–99.\nNuengchamnong, N., K. Ingkaninan, W. Kaewruang, S. Wongareonwanakij, and B. Hongthongdaeng (2007) Quantitative determination of 1-deoxynojirimycin in mulberry leaves using liquid chromatography-tandem mass spectrometry. J. Pharm. Biomed. Anal. 44: 853–858.\nKimura, T., K. Nakagawa, Y. Saito, K. Yamagishi, M. Suzuki, K. Yamaki, H. Shinmoto, and T. Miyazawa (2004) Determination of 1-deoxynojirimycin in mulberry leaves using hydrophilic interaction chromatography with evaporative light scattering detection. J. Agric. Food Chem. 52: 1415–1418.\nRooney, A. P., N. P. Price, C. Ehrhardt, J. L. Swezey, and J. D. Bannan (2009) Phylogeny and molecular taxonomy of the Bacillus subtilis species complex and description of Bacillus subtilis subsp. inaquosorum subsp. nov. Int. J. Syst. Evol. Microbiol. 59: 2429–2436.\nYi, H., J. Chun, and C. J. Cha (2014) Genomic insights into the taxonomic status of the three subspecies of Bacillus subtilis. Syst. Appl. Microbiol. 37: 95–99.\nRegmi S., H. Y. Yoo, Y. H. Choi, Y. S. Choi, J. C. Yoo, and S. W. Kim (2017) Prospects for bio-industrial application of an extremely alkaline mannanase from Bacillus subtilis subsp. inaquosorum CSB31. Biotechnol. J. 12: 1700113.\nKnight, C. A., M. J. Bowman, L. Frederick, A. Day, C. Lee, and C. A. Dunlap (2018) The first report of antifungal lipopeptide production by a Bacillus subtilis subsp. inaquosorum strain. Microbiol. Res. 216: 40–46.\nBapiraju, K. V. V. S. N., P. Sujatha, P. Ellaiah, and T. Ramana (2004) Mutation induced enhanced biosynthesis of lipase. Afr. J. Biotechnol. 3: 618–621.\nOnose, S., R. Ikeda, K. Nakagawa, T. Kimura, K. Yamagishi, O. Higuchi, and T. Miyazawa (2013) Production of the α-glycosidase inhibitor 1-deoxynojirimycin from Bacillus species. Food Chem. 138: 516–523.\nSeo, M. J., Y. D. Nam, S. Y. Lee, S. L. Park, S. H. Yi, and S. I. Lim (2013) Isolation of the putative biosynthetic gene cluster of 1-deoxynojirimycin by Bacillus amyloliquefaciens 140N, its production and application to the fermentation of soybean paste. Biosci. Biotechnol. Biochem. 77: 398–401.\nPaek, N. S., D. J. Kang, Y. J. Choi, J. J. Lee, T. H. Kim, and K. W. Kim (1997) Production of 1-deoxynojirimycin by Streptomyces sp. SID9135. J. Microbiol. Biotechnol. 7: 262–266.",{"VOID":217},"10.1007\u002Fs12257-020-0231-2","PUBLICATION","VERIFIED","2024-12-24T22:11:45.141+00:00","Auto Verify",[223],"VI","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12257-020-0231-2",[226,251,271,292,312,333,353],{"id":227,"sortIndex":21,"researcher":20,"roles":228,"affiliations":230,"properties":248,"displayName":250,"givenName":20,"familyName":20},"b3192d37-7d4e-4b49-9686-05ccb83d5861",[229],"AUTHOR",[231,239],{"id":232,"sortIndex":21,"affiliation":233,"properties":20},"155ba4a1-86cc-4ada-b0e5-f5960b80ea19",{"id":232,"createTime":20,"updateTime":20,"relativeEntities":234,"slug":20,"properties":235,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":238,"statistic":20},[],{"title":236},{"VI":237},"Environmental Disease Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea",[],{"id":240,"sortIndex":172,"affiliation":241,"properties":247},"25cc5895-e19f-4db7-9dcd-6457df98f466",{"id":240,"createTime":20,"updateTime":20,"relativeEntities":242,"slug":20,"properties":243,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":246,"statistic":20},[],{"title":244},{"VI":245},"Department of Biosystems and Bioengineering, KRIBB School of Biotechnology, University of Science and Technology (UST), Daejeon, Korea",[],{},{"title":249},{"VI":250},"Khai Ngoc 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this study, optimization of ultrasound-assisted extraction (UAE) conditions was conducted to increase the production of bioactive components from Carthamus tinctorius seeds (CS) using statistically-based optimization. The effects of major independent variables including extraction time (5.0–55.0 min), extraction temperature (26.0–94.0°C), and ethanol concentration (0.0–99.5%) were optimized using central composite design (CCD) to explore conditions that simultaneously maximize total polyphenol content, total flavonoid content, and radical scavenging activity. According to quadratic regression models, the predicted optimum UAE conditions were 33.7 min, 75.1°C, and 68.3% ethanol, respectively. Under these conditions, the experimental results were found to be 9.94 mg gallic acid equivalents\u002Fg dry matter (DM) of TPC, 0.28 mg quercetin equivalents\u002Fg DM of TFC, and 66.6% of RSA which are in good agreement with the predicted values. CS extract was subjected to LC\u002FMS\u002FMS analysis to analyze components with bioactive activities, and apigenin was determined as the main component. Therefore, we have concluded that UAE is an effective process for extracting antioxidant components and CS extract with bioactive components can be utilized as food, cosmetics, and pharmaceutical materials.",{"EN":451,"VI":452},"Ultrasound-assisted Extraction of Polyphenols from Carthamus tinctorius Seeds: Optimization of Process Variables","Chiết xuất polyphenol từ hạt Carthamus tinctorius có hỗ trợ của sóng siêu âm: Tối ưu hóa các biến quy trình",{"VOID":454},"Xu, D., D. Liu, B. Wang, C. Chen, Z. Chen, D. Li, Y. Yang, H. Chen, and M. G. Kong (2015) In situ OH generation from O2− and H2O2 plays a critical role in plasma-induced cell death. PLoS One 10: e0128205.\nLi, R., Z. Jia, and M. A. Trush (2016) Defining ROS in biology and medicine. React. Oxyg. Species (Apex) 1: 9–21.\nOnukwufor, J. O., B. J. Berry, and A. P. Wojtovich (2019) Physiologic implications of reactive oxygen species production by mitochondrial complex I reverse electron transport. Antioxidants (Basel) 8: 285.\nChoi, S. J., E. Cho, E. Cho, Y. Jeong, C. S. Ku, B. Ha, and H. J. Chae (2011) Screening of functional materials from solvent fractions of apple flower leaf extract. Korean Soc. Biotechnol. Bioeng. J. 26: 165–171.\nKovac, S., P. R. Angelova, K. M. Holmström, Y. Zhang, A. T. Dinkova-Kostova, and A. Y. Abramov (2015) Nrf2 regulates ROS production by mitochondria and NADPH oxidase. Biochim. Biophys. Acta 1850: 794–801.\nForrester, S. J., D. S. Kikuchi, M. S. Hernandes, Q. Xu, and K. K. Griendling (2018) Reactive oxygen species in metabolic and inflammatory signaling. Circ. Res. 122: 877–902.\nSim, H., Y. Noh, S. Choo, N. Kim, T. Lee, and J. S. Bae (2021) Suppressive activities of fisetin on particulate matter-induced oxidative stress. Biotechnol. Bioprocess Eng. 26: 568–574.\nJeong, M. J., D. S. Lim, S. O. Kim, C. Park, S. H. Leem, H. Lee, G. Y. Kim, S. J. Jeong, and Y. H. Choi (2022) Protection of oxidative stress-induced DNA damage and apoptosis by rosmarinic acid in murine myoblast C2C12 cells. Biotechnol. Bioprocess Eng. 27: 171–182.\nDing, M. and J. Zou (2012) Rapid micropreparation procedure for the gas chromatographic-mass spectrometric determination of BHT, BHA and TBHQ in edible oils. Food Chem. 131: 1051–1055.\nNasirullah and R. B. Latha (2009) Storage stability of sunflower oil with added natural antioxidant concentrate from sesame seed oil. J. Oleo Sci. 58: 453–459.\nYoon, J. H., S. G. Park, M. J. Lee, J. Y. Park, K. S. Seo, K. C. Woo, and C. E. Lee (2013) Antioxidant and anti-inflammatory effects of Bletilla striata Reichenbach fil. fractions as cosmetic. J. Life Sci. 23: 1073–1078.\nKang, M. C., W. W. Lee, J. Y. Oh, H. S. Kim, H. G. Lee, and Y. J. Jeon (2017) Thermostability of Ecklonia cava extract on antioxidant activity. J. Mar. Biosci. Biotechnol. 9: 43–48.\nPark, S. J., S. W. Song, D. H. Seong, D. S. Park, S. S. Kim, J. Gou, J. H. Ahn, W. B. Yoon, and H. Y. Lee (2009) Biological activities in the extract of fermented Codonopsis lanceolata. J. Korean Soc. Food Sci. Nutr. 38: 983–988.\nKim, J., K. Lee, and Y. S. Nam (2021) Metal-polyphenol complexes as versatile building blocks for functional biomaterials. Biotechnol. Bioprocess Eng. 26: 689–707.\nLee, K. J. and B. H. Um (2008) Extraction of useful component from natural plants using ultrasound system. Korean J. Biotechnol. Bioeng. 23: 101–108.\nLee, K. J., J. Y. Ma, and Y. S. Kim (2012) Identification of curcuminoids from turmeric (Curcuma longa) using ultrasonic wave and dipping method. Korean Soc. Biotechnol. Bioeng. J. 27: 33–39.\nLee, K. J., H. J. Yang, S. W. Jeong, and J. Y. Ma (2012) Solid-phase extraction of curcuminoid from turmeric using physical process method. Korean J. Pharmacogn. 43: 250–256.\nWen, C., J. Zhang, H. Zhang, C. S. Dzah, M. Zandile, Y. Duan, H. Ma, and X. Luo (2018) Advances in ultrasound assisted extraction of bioactive compounds from cash crops - a review. Ultrason. Sonochem. 48: 538–549.\nKhan, M. A., S. von Witzke-Ehbrecht, B. L. Maass, and H. C. Becker (2009) Relationships among different geographical groups, agro-morphology, fatty acid composition and RAPD marker diversity in safflower (Carthamus tinctorius). Genet. Resour. Crop Evol. 56: 19–30.\nZemour, K., A. Labdelli, A. Adda, A. Dellal, T. Talou, and O. Merah (2019) Phenol content and antioxidant and antiaging activity of safflower seed oil (Carthamus tinctorius L.). Cosmetics 6: 55.\nDelshad, E., M. Yousefi, P. Sasannezhad, H. Rakhshandeh, and Z. Ayati (2018) Medical uses of Carthamus tinctorius L. (Safflower): a comprehensive review from Traditional Medicine to Modern Medicine. Electron. Physician 10: 6672–6681.\nHidayat, M. A., D. A. Maharani, D. A. Purwanto, B. Kuswandi, and M. Yuwono (2020) Simple and sensitive paper-based colorimetric biosensor for determining total polyphenol content of the green tea beverages. Biotechnol. Bioprocess Eng. 25: 255–263.\nRuslan, K., S. Happyniar, and I. Fidrianny (2018) Antioxidant potential of two varieties of Sesamum indicum L. collected from Indonesia. J. Taibah Univ. Med. Sci. 13: 211–218.\nKim, H., Y. Jeong, J. E. Kim, Y. G. Kim, N. S. Paek, and C. H. Kang (2021) Anti-obesity potential of Lactobacillus spp. isolated from infant feces. Biotechnol. Bioprocess Eng. 26: 575–585.\nMin, D. L., S. Lim, J. B. Ahn, and Y. J. Choi (2010) Optimization of ethanol extraction conditions for antioxidants from Zizyphus jujuba Mill. leaves using response surface methodology. Korean J. Food Sci. Technol. 42: 733–738.\nJo, I. H., C. Y. Kim, T. W. Lee, G. H. Lee, and Y. H. Choi (2010) Optimization of extraction of effective components from Vitis coignetiae, the crimson glory vine. Korean J. Food Preserv. 17: 659–666.\nKim, S. H., I. H. Kim, B. H. Kang, K. H. Lee, S. H. Lee, D. S. Lee, S. K. Cho, S. S. Hur, T. K. Kwon, and J. M. Lee (2009) Optimization of ethanol extraction conditions from propolis (a bee product) using response surface methodology. Korean J. Food Preserv. 16: 908–914.\nKoh, Y. J., D. S. Cha, H. D. Choi, Y. K. Park, and I. W. Choi (2008) Hot water extraction optimization of dandelion leaves to increase antioxidant activity. Korean J. Food Sci. Technol. 40: 283–289.\nPark, M. G. and S. Y. Joo (2021) Comparison of antioxidant activities of sea buckthorn (Hippophae rhamnoides) leaf extracts at different ethanol ratios. Korean J. Food Sci. Technol. 53: 55–62.\nPark, S. J. (2019) Antioxidant activities and whitening effects of ethanol extract from Panax ginseng sprout powder. J. Korean Soc. Food Sci. Nutr. 48: 276–281.\nLee, E. K., H. G. Hong, and M. S. Chong (2009) Study on the comparison of effects by extraction methods of roast and raw semen zizyphi spinosae. Korean J. Orient. Physiol. Pathol. 23: 1416–1422.\nMin, B. R., Y. J. Han, D. K. Lee, H. J. Jung, J. M. Jo, and J. W. Kim (2018) Optimization of microwave-assisted extraction conditions for production of bioactive material from corn stover. Korean Chem. Eng. Res. 56: 66–72.\nWoo, K. S., S. B. Song, B. G. Oh, M. C. Seo, J. Y. Ko, J. S. Lee, J. R. Kang, M. H. Nam, and H. S. Jeon (2009) Antioxidant activity of ethanol extracts from horseweed (Erigeron canadensis L.) with pretreatment conditions. J. Korean Soc. Food Sci. Nutr. 38: 1279–1283.\nChung, K.H. and B.G. Park (2013) Biodiesel production from waste oils mixed with animal tallows and vegetable oil by transesterification using ultrasonic irradiation. Korean Chem. Eng. Res. 51: 487–492.\nKim, D. I. and J. H. Hong (2012) Optimization of ethanol extraction conditions for functional components from Lespedeza cuneata using response surface methodology. Korean J. Food Cook. Sci. 28: 275–283.\nShin, Y. J., J. M. Hwang, and S. C. Lee (2013) Antioxidant and xanthine oxidase inhibitory activities of hot water extracts of medicinal herbs. J. Korean Soc. Food Sci. Nutr. 42: 1712–1716.\nKim, H. Y., K. S. Woo, I. G. Hwang, Y. R. Lee, and H. S. Jeong (2008) Effects of heat treatments on the antioxidant activities of fruits and vegetables. Korean J. Food Sci. Technol. 40: 166–170.\nKang, K. J., B. H. Kim, D. Kim, H. J. Yun, Y. S. Cho, N. E. Han, J. C. Choi, S. Lee, and O. K. Choi (2021) Determination of the contents of apigenin and luteolin in vegetables. Korean J. Food Nutr. 34: 233–241.\nHuang, W. Y., Y. Z. Cai, and Y. Zhang (2009) Natural phenolic compounds from medicinal herbs and dietary plants: potential use for cancer prevention. Nutr. Cancer 62: 1–20.\nBrglez Mojzer, E., M. Knez Hrnčič, M. Škerget, Ž. Knez, and U. Bren (2016) Polyphenols: extraction methods, antioxidative action, bioavailability and anticarcinogenic effects. Molecules 21: 901.",{"VOID":456},"10.1007\u002Fs12257-022-0092-y","2024-12-18T17:56:47.199+00:00",[223],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12257-022-0092-y",[461,476,489,502,515],{"id":462,"sortIndex":21,"researcher":20,"roles":463,"affiliations":464,"properties":473,"displayName":475,"givenName":20,"familyName":20},"f7bfec13-86f3-464f-90d3-3699a4604b65",[229],[465],{"id":466,"sortIndex":21,"affiliation":467,"properties":20},"4366e51d-d5db-4442-9da6-51ae884ac692",{"id":466,"createTime":20,"updateTime":20,"relativeEntities":468,"slug":20,"properties":469,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":472,"statistic":20},[],{"title":470},{"EN":471},"Department of Food Science, Sun Moon University, Asan, Korea",[],{"title":474},{"VI":475},"Jun Hee 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Food Eng. 77: 880–886.",{"doi":838},"10.1016\u002Fj.jfoodeng.2005.08.016",{"id":840,"createTime":841,"updateTime":842,"relativeEntities":843,"slug":844,"properties":845,"entityType":218,"verifyStatus":219,"verifyTime":856,"verifyNote":221,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":857,"fullTextUrl":20,"authors":858,"publicationType":376,"publisherRelationship":985,"citationCount":21,"citationInfo":1045,"publishDate":1048,"publishYear":1046,"citationAnalyzeStatus":749,"lastCitationAnalyze":842,"indexDatabases":1049,"openAccess":20,"references":20,"isForceReanalyzing":440},"c27e18b5-7553-4b35-80e1-6dd13c8dca3a","2023-12-25T17:49:26.834+00:00","2026-08-16T04:20:15.433+00:00",[],"Ectopic-Overexpression-of-Teff-Grass-Eragrostis-tef-Phi-class-Glutathione-S-transferase-1-EtGSTF1-Enhances-Prokaryotic-Cell-Survivability-against-Diverse-Abiotic-Stresses",{"abstract":846,"title":848,"gsPaper":850,"references":852,"doi":854},{"EN":847},"The glutathione S-transferases (GSTs) are encoded by a large gene family and well conserved in all living organisms; however they have evolved and are classified clearly according to each kingdom. GSTs are a dimeric protein that has been reported to maintain redox homeostasis in cells, and to protect organisms against oxidative damage. Recently, we isolated a GST coding gene from stress-treated teff grass (Eragrostis tef) and identified it as a plant-specific phi class GST (EtGSTF1) possessing conserved phi class-specific GST N- and C-terminal domains, GSH binding site, substrate binding pocket, and dimer interface. We found that overexpression of plant-specific phi class EtGSTF1 confers diverse abiotic stress tolerances including salt, osmotic, and heat stresses in E. coli which does not possess phi class GSTs. In addition, EtGSTF1 expression helps the E. coli cells tolerate arsenic (As)-induced cell toxicity. Collectively, although plantae and prokaryotae have differentiated a few billions of years ago, the plant-specific phi class EtGSTF1 could protect prokaryotic organisms by detoxification of molecules under diverse abiotic stresses.",{"EN":849},"Ectopic Overexpression of Teff Grass (Eragrostis tef) Phi-class Glutathione S-transferase 1 (EtGSTF1) Enhances Prokaryotic Cell Survivability against Diverse Abiotic Stresses",{"VOID":851},"[\"1721762722585337501\"]",{"VOID":853},"Pompella, A., A. Visvikis, A. Paolicchi, V. D. Tata, and A. F. Casini (2003) The changing faces of glutathione, a cellular protagonist. Biochem. Pharmacol. 66: 1499–1503.\nCouto, N., N. Malys, S. J. Gaskell, and J. Barber (2013) Partition and turnover of glutathione reductase from Saccharomyces cerevisiae: a proteomic approach. J. Proteome Res. 12: 2885–2894.\nPastore, A., F. Piemonte, M. Locatelli, A. Lo Russo, L. M. Gaeta, G. Tozzi, and G. Federici (2001) Determination of blood total, reduced, and oxidized glutathione in pediatric subjects. Clinical Chem. 47: 1467–1469.\nWilce, M. C. J., and M. W. Parker (1994) Structure and function of glutathione S-transferases. Biochim. Biophys. Acta. 1205: 1–18.\nMiller, G., N. Suzuki, S. Ciftci-Yilmaz, and R. Mittler (2010) Reactive oxygen species homeostasis and signalling during drought and salinity stresses. Plant Cell Environ. 33: 453–467.\nGallé, Á., Z. Czékus, K. Bela, E. Horváth, A. Ördög, J. Csiszár, and P. Poór (2019) Plant glutathione transferases and light. Front. Plant Sci. 9:1944.\nLai, A. G., C. J. Doherty, B. Mueller-Roeber, S. A. Kay, J. H. M. Schippers, and P. P. Dijkwel (2012) Circadian clock-associated 1 regulates ROS homeostasis and oxidative stress responses. Proc. Natl. Acad. Sci. USA. 109: 17129–17134.\nGechev, T. S., F. Van Breusegem, J. M. Stone, I. Denev, and C. Laloi (2006) Reactive oxygen species as signals that modulate plant stress responses and programmed cell death. Bioessays. 28: 1091–1101.\nDixon, D. P., A. Lapthorn, and R. Edwards (2002) Plant glutathione transferases. Genome Biol. 3: 3004.\nMukanganyama, S., M. Bezabih, M. Robert, B. T. Ngadjui, G. F. W. Kapche, F. Ngandeu, and B. Abegaz (2011) The evaluation of novel natural products as inhibitors of human glutathione transferase P1-1. J. Enzyme Inhib. Med. Chem. 26: 460–467.\nAllocati, N., L. Federici, M. Masulli, and C. Di Ilio (2009) Glutathione transferases in bacteria. FEBS. J. 276: 58–75.\nMarrs, K. A. (1996) The functions and regulation of glutathione s-transferases in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47: 127–158.\nChronopoulou, E., N. Georgakis, I. Nianiou-Obeidat, P. Madesis, F. Perperopoulou, F. Pouliou, E. Vasilopoulou, E. Ioannou, F. S. Ataya, and N. E. Labrou (2017) Plant glutathione transferases in abiotic stress response and herbicide resistance. In: Hossain, M.A., Mostofa, M.G., Diaz-Vivancos, P., Burritt, D.J., Fujita, M., Tran, L.S.P. (Eds.), Glutathione in plant growth, development, and stress tolerance. Springer International Publishing, Cham. pp. 215–233.\nNianiou-Obeidat, I., P. Madesis, C. Kissoudis, G. Voulgari, E. Chronopoulou, A. Tsaftaris, and N. E. Labrou (2017) Plant glutathione transferase-mediated stress tolerance: functions and biotechnological applications. Plant Cell Rep. 36: 791–805.\nDixon, D. P., I. Cummins, D. J. Cole, and R. Edwards (1998) Glutathione-mediated detoxification systems in plants. Curr. Opin. Plant Biol. 1: 258–266.\nHu, T. (2014) A glutathione s-transferase confers herbicide tolerance in rice. Crop Breed.Appl.Biot. 14: 76–81.\nKim, Y.-O., H.-J. Bae, E. Cho, and H. Kang (2017) Exogenous glutathione enhances mercury tolerance by inhibiting mercury entry into plant cells. Front. Plant Sci. 8:683.\nKumar, S., and P. K. Trivedi (2018) Glutathione S-transferases: role in combating abiotic stresses including arsenic detoxification in plants. Front. Plant Sci. 9:751.\nLiu, S.-H., G.-M. Zeng, Q.-Y. Niu, Y. Liu, L. Zhou, L.-H. Jiang, X.-f. Tan, P. Xu, C. Zhang, and M. Cheng (2017) Bioremediation mechanisms of combined pollution of PAHs and heavy metals by bacteria and fungi: a mini review. Bioresource Technol. 224: 25–33.\nShehu, D., N. Abdullahi, and Z. Alias (2019) Cytosolic glutathione S-transferase in bacteria: a review. Pol. J. Environ. Stud. 28: 515–528.\nZablotowicz, R. M., R. E. Hoagland, M. A. Locke, and W. J. Hickey (1995) Glutathione-s-transferase activity and metabolism of glutathione conjugates by rhizosphere bacteria. Appl. Environ. Microbiol. 61: 1054–1060.\nKunieda, T., T. Fujiwara, T. Amano, and Y. Shioi (2005) Molecular cloning and characterization of a senescence-induced tau-class glutathione s-transferase from barley leaves. Plant Cell Physiol. 46: 1540–1548.\nDavidson, J. M., D. Min, RM. Aiken, and G.J.Kluitenberg (2018) Evaluating teff grass as a summer forage. Kansas Agricultural Experiment Station Research Reports, USA. pp. 1–5.\nLee, K., M. A. Rahman, G. Choi, H. Ji, T. Hwang, and S. Lee (2018) Identification of differentially expressed abiotic stress-induced genes in teff grass (Eragrostis tef) leaves. JAPS 28: 1189–1193.\nLee, S.-H., K.-W. Lee, D.-G. Lee, D. Son, S. J. Park, K.-Y. Kim, H. S. Park, and J.-Y. Cha (2015) Identification and functional characterization of Siberian wild rye (Elymus sibiricus L.) small heat shock protein 16.9 gene (EsHsp16.9) conferring diverse stress tolerance in prokaryotic cells. Biotechnol. Lett. 37: 881–890.\nEaton, D. L., and T. K. Bammler (1999) Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol. Sci. 49: 156–164.\nOakley, A. (2011) Glutathione transferases: a structural perspective. Drug Metab.Rev. 43: 138–151.\nSheehan, D., G. Meade, V. M. Foley, and C. A. Dowd (2001) Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360: 1–16.\nFrova, C. (2006) Glutathione transferases in the genomics era: New insights and perspectives. Biomol. Eng. 23: 149–169.\nAllocati, N., B. Favaloro, M. Masulli, M. F. Alexeyev, and C. Di Ilio (2003) Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses. Biochem. J. 373: 305–311.\nLee, K.-W., M. A. Rahman, K.-Y. Kim, G. J. Choi, J.-Y. Cha, M. S. Cheong, A. M. Shohael, C. Jones, and S.-H. Lee (2018) Overexpression of the alfalfa DnaJ-like protein (MsDJLP) gene enhances tolerance to chilling and heat stresses in transgenic tobacco plants. Turk. J. Biol. 42: 12–22.\nHossain, M., M. R. Ismail, M. K. Uddin, M. Islam, and M. Ashrafuzzaman (2013) Efficacy of ascorbate-glutathione cycle for scavenging H2O2 in two contrasting rice genotypes during salinity stress. Aus. J.Crop Sci. 7: 1801–1808.\nPyngrope, S., K. Bhoomika, and R. S. Dubey (2013) Reactive oxygen species, ascorbate-glutathione pool, and enzymes of their metabolism in drought-sensitive and tolerant indica rice (Oryza sativa L.) seedlings subjected to progressing levels of water deficit. Protoplasma. 250: 585–600.\nRyu, H. Y., S. Y. Kim, H. M. Park, J. Y. You, B. H. Kim, J. S. Lee, and K. H. Nam (2009) Modulations of AtGSTF10 expression induce stress tolerance and BAK1-mediated cell death. Biochem. Biophys. Res. Commun. 379: 417–422.\nChen, J.-H., H.-W. Jiang, E.-J. Hsieh, H.-Y. Chen, C.-T. Chien, H.-L. Hsieh, and T.-P. Lin (2012) Drought and salt stress tolerance of an Arabidopsis glutathione S-transferase U17 knockout mutant are attributed to the combined effect of glutathione and abscisic acid. Plant Physiol. 158: 340–351.\nKumar, S., R. S. Dubey, R. D. Tripathi, D. Chakrabarty, and P. K. Trivedi (2015) Omics and biotechnology of arsenic stress and detoxification in plants: current updates and prospective. Environ. Int. 74: 221–230.\nSharma, I. (2012) Arsenic induced oxidative stress in plants. Biologia. 67: 447–453.\nRahman, M. A., S.-H. Lee, K.-Y. Kim, H. S. Park, T. Y. Hwang, G. J. Choi, and K.-W. Lee (2016) Arsenic-induced differentially expressed genes identified in Medicago sativa L. roots. J. Korean Soc. Grassl. 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addition of a limited concentration of yeast extract to a minimal salt medium (MSM) enhanced cell growth and increased the production of curdlan whereas nitrogenlimitation was found to be essential for the higher production of curdlan byAgrobacterium sp. ATCC 31749. As the amount of the inoculum increased, the cell growth as well as the production of curdlan also increased in the MSM without a nitrogen source. The cell growth and production of curdlan increased as the initial pH of the medium decreased as low as 5.0. The conversion rate and concentration of curdlan from 2% (w\u002Fv) glucose in the MSM with concentrated cells under nitrogen deletion was 67% and 13.4 g\u002FL, respectively. The highest conversion rate of curdlan under the conditions optimized in this study was 71% when the glucose concentration was 1% (w\u002Fv).",{"EN":1060},"Improved production of curdlan with concentrated cells ofAgrobacterium sp.",{"VOID":1062},"[\"13965953341327251940\"]",{"VOID":1064},"Harada, T., K. Fujimori, S. Hirose, and M. Masada (1966) Crowth and β-1,3 glucan 10C3K production by a mutant ofAlcaligenes faecalis var.myxogenes in defined medium.Agr. Biol. Chem. 30: 764–769.\nHarada, T., A. Misaki, and H. Saito (1968) Curdlan: A bacterialgel-forming β-1,3-glucan.Arch. Biochem. 124: 292–298.\nMaeda, I., H. Saito, M. Masada, A. Misaki, and T. Harada (1967) Properties of gels formed by heat treatment of curdlan, a bacterial β-1,3 glucan.Agr. Biol. Chem. 31: 1184–1188.\nHarada, T., M. Masada, K. Fujimori, and I. Maeda (1966) Production of a firm, resilient gel-forming polysaccharide by a mutant ofAlcaligenes faecalis var.myxogenes 10C3.Agr. Biol. Chem. 30: 196–198.\nAyers, S. H. and P. Rupp (1920) Extracts of pure dry yeast for culture media.J. Bacteriol. 5: 89–98.\nHarada, T., M. Masada, K. Fujimori, and I. Maeda (1966) Production of firm, resilient gel-forming polysaccharide in natural medium by a mutant ofAlcaligenes faecalis var.myxogenes 10C3.J. Ferment. Technol. 44: 20–24.\nPhillips, K. R. and H. C. Lawford (1983) Curdlan: its properties and production in batch and continuous fermentation.Prog. Ind. Microbiol. 18: 201–229.\nLawford, H. G., K. R. Phillips, and G. R. Lawford (1982) A two stage continuous process for the production of thermogelable curdlan-type expolysaccharide.Biotechnol. Lett. 4: 689–694.\nLee, I. Y., W. T. Seo, G. J. Kim, C. S. Park, and Y. H. Park (1997) Production of curdlan of using sucrose or sugar cane molasses by two-step fed-batch cultivation ofAgrobacterium species.J. Ind. Microbiol. Biotechnol. 18: 255–259.\nSeviour, R. J. and B. Kristiansen (1983) Effect of ammonium ion concentration on polysaccharide production byAureobasidium pullulans in batch culture.Eur. J. Appl. Microbiol. Biotechnol. 17: 178–181.\nKo, S. H., H. S. Lee, S. H. Park, and H. K. Lee (2000) Optimal conditions for the production of exopolysaccharide by marine microorganismHahella chejuensis.Biotechnol. Bioprocess Eng. 5: 181–185.\nOrts, W. J., J. D. Rousseau, and H. G. Lawfor ((1987) Improved microbial production of curdlan type-polysaccharide. pp. 459–469. In: S. Stivala, V. Crescenzi, and I. C. M. Dea (eds.).Industrial Polysaccharides. Gordon Breach Science, New York, USA.\nPhillips, K. R., J. Pik, H. G. Lawford, B. Lavers, A. Kligerman, and G. R. Lawford (1983) Production of curdlantype polysaccharide byAlcaligenes faecalis in batch and continuous culture.Can. J. Microbiol. 29: 1331–1338.\nLawford, H. G. (1982) Continuous process for the production of gelable exopolysaccharide.US Patent 4,355,106.\nLawford, H. G. and J. D. Rousseau (1992) Production of β-1,3-glucan exopolysaccharide in low shear systems.Appl. Biochem. Biotechnol. 34\u002F35: 597–612.\nLee, J. W., W. G. Yeomans, A. F. Allen, D. L. Kaplan, F. Deng, and R. A. Gross (1997) Exopolymers from curdlan production: incorporation of glucose-related sugars byAgrobacterium sp. strain ATCC 31749.Can. J. Microbiol. 43: 149–156.\nLee, J. W., W. G. Yeomans, A. F. Allen, D. L. Kaplan, and R. A. Gross (1997) Microbial production of water-soluble non curdlan type exopolymer-B with controlled composition byAgrobacterium sp.Biotechnol. Lett. 19: 1217–1221.\nChaplin, M. (1982) A rapid and sensitive method for the analysis of carbohydrate components in glycoproteins using gas-liquid chromatography.Anal. Biochem. 123: 336–341.\nSharmila, M., K. Ramanans, and N. Sethunathan (1989) Effect of yeast extract on the degradation of organophosphorous insecticides by soil enrichment and bacterial cultures.Can. J. Microbiol. 35: 1105–1110.\nShen, C. F., N. Kosaric, and R. Blaszezyk (1993) Properties of anaerobic sludge as affected by yeast extract, cobalt and iron suppleents.Appl. Microbiol. Biotechnol. 39: 132–137.\nKim, M. K., I. Y. Lee, J. H. Ko, Y. H. Rhee, and Y. H. Park (1999) Higher intracellular levels of uridinemonophosphate under nitrogen-limited conditions enhance metabolic flux of curdlan synthesis inAgrobacterium species.Biotechnol. Bioeng. 62: 317–323.\nEbbole, D. J. (1998) Carbon catabolite repression of gene expression and condition inNeurospora crassa.Fungal Gen. Biol. 25: 15–21.\nAnwar, M. N., M. Suto, and F. Tomita (1996) Isolation of mutants ofPenicillium purpurogen resistant to catabolite repression.Appl. Microbiol. Biotechnol. 45: 684–687.\nWolff, J. A., C. H. MacGregor, R. C. Eisenberg, and P. V. Phibbs Jr. (1991) Isolation and characterization of catabolite repression control mutants ofPseudomonas acruginosa PAO.J. Bacteriol. 173: 4700–4706.\nGancedo, J. M. (1998) Yeast carbon catabolite repression.Microbiol. Mol. Biol. Rev. 62: 334–361.\nLee, I. Y., M. K. Kim, W. T. Lee, J. K. Seo, H. W. Jung, and Y. H. Park (1999) Influence of agitation speed on production of curdlan byAgrobacterium species.Bioproess Eng. 20: 283–287.",{"VOID":1066},"10.1007\u002FBF02931955","2024-06-25T15:29:19.052+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02931955",[1070,1085,1098,1111,1126,1141],{"id":1071,"sortIndex":21,"researcher":20,"roles":1072,"affiliations":1073,"properties":1082,"displayName":1084,"givenName":20,"familyName":20},"e29d13e4-7bd3-45ef-b59e-1bc2d6612afe",[229],[1074],{"id":1075,"sortIndex":21,"affiliation":1076,"properties":20},"d8c7028a-bbcb-49bf-9772-51312d6f4b4b",{"id":1075,"createTime":20,"updateTime":20,"relativeEntities":1077,"slug":20,"properties":1078,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1081,"statistic":20},[],{"title":1079},{"VI":1080},"Division of Biotechnology, Faculty of Natural Resources and Life Science, Dong-A University, Pusan, Korea",[],{"title":1083},{"VI":1084},"Dae-Young Jung",{"id":1086,"sortIndex":172,"researcher":20,"roles":1087,"affiliations":1088,"properties":1095,"displayName":1097,"givenName":20,"familyName":20},"5d92b27f-1d94-4cfc-b307-4b0ba193b787",[229],[1089],{"id":1075,"sortIndex":21,"affiliation":1090,"properties":20},{"id":1075,"createTime":20,"updateTime":20,"relativeEntities":1091,"slug":20,"properties":1092,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1094,"statistic":20},[],{"title":1093},{"VI":1080},[],{"title":1096},{"VI":1097},"Young-Su Cho",{"id":1099,"sortIndex":273,"researcher":20,"roles":1100,"affiliations":1101,"properties":1108,"displayName":1110,"givenName":20,"familyName":20},"823bc705-e68f-43aa-abe8-8fe2bc1222a8",[229],[1102],{"id":1075,"sortIndex":21,"affiliation":1103,"properties":20},{"id":1075,"createTime":20,"updateTime":20,"relativeEntities":1104,"slug":20,"properties":1105,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1107,"statistic":20},[],{"title":1106},{"VI":1080},[],{"title":1109},{"VI":1110},"Chung-Han Chung",{"id":1112,"sortIndex":171,"researcher":20,"roles":1113,"affiliations":1114,"properties":1123,"displayName":1125,"givenName":20,"familyName":20},"c65c13ca-d752-46e1-93a2-4e726ddacac0",[229],[1115],{"id":1116,"sortIndex":21,"affiliation":1117,"properties":20},"d2501045-42eb-4cc9-851c-b2b8af0cfab2",{"id":1116,"createTime":20,"updateTime":20,"relativeEntities":1118,"slug":20,"properties":1119,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1122,"statistic":20},[],{"title":1120},{"VI":1121},"Deperatment of Chemistry, College of Natural Science, Dong-A University, Pusan, Korea",[],{"title":1124},{"VI":1125},"Dai-Il Jung",{"id":1127,"sortIndex":314,"researcher":20,"roles":1128,"affiliations":1129,"properties":1138,"displayName":1140,"givenName":20,"familyName":20},"3747fafb-f2d9-49da-aae2-500b37c64378",[229],[1130],{"id":1131,"sortIndex":21,"affiliation":1132,"properties":20},"0544633d-09bb-4f6c-b7cf-a7b320bfdc6c",{"id":1131,"createTime":20,"updateTime":20,"relativeEntities":1133,"slug":20,"properties":1134,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1137,"statistic":20},[],{"title":1135},{"VI":1136},"Department of Chemical EngIneering College of EngIneering, Dong-A University, Pusan, Korea",[],{"title":1139},{"VI":1140},"Kwang Kim",{"id":1142,"sortIndex":146,"researcher":20,"roles":1143,"affiliations":1144,"properties":1151,"displayName":1153,"givenName":20,"familyName":20},"ba7b6a58-7b02-4bc2-922b-937d60058930",[229],[1145],{"id":1075,"sortIndex":21,"affiliation":1146,"properties":20},{"id":1075,"createTime":20,"updateTime":20,"relativeEntities":1147,"slug":20,"properties":1148,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1150,"statistic":20},[],{"title":1149},{"VI":1080},[],{"title":1152},{"VI":1153},"Jin-Woo 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large-scale production of functional recombinant lactoferrin has become a major goal because of its medicinal value and global demand. Secreting recombinant proteins into a culture medium offers a way to simplify protein purification and avoid toxicity from intracellularly accumulated materials. In this study, after 84 h of induction with methanol in a shaking flask, the recombinant bovine lactoferrin (rbLf) titer in the culture supernatant of the strain that integrated two copies of the rbLf gene was only 121.6 μg\u002FL. A bottleneck might have existed in the folding and secretion pathways of rbLf. We then attempted to further improve the rbLf titer by overexpressing the transcription factor Haclp and α-signal peptide-cutting protease Kex2p with different promoters. Results showed that the inducible coexpression of Haclp and Kex2p linked with the 2A sequence improved the rbLf titer 5.0-fold (735.8 μg\u002FL) after 84 h of induction with methanol. The maximal titer in a shaking flask was 1,150.5 μg\u002FL after 120 h of induction. The rbLf titer achieved 35.6 mg\u002FL in a 5 L fed-batch fermenter. Thus, Kex2 and Hacl overexpression driven by methanol-induced promoter alleviated the bottleneck in the folding and secretion pathways and greatly improved the secretory expression of rbLf in Pichia pastoris.",{"EN":1230},"Coexpression of Kex2 Endoproteinase and Hac1 Transcription Factor to Improve the Secretory Expression of Bovine Lactoferrin in Pichia pastoris",{"VOID":1232},"[\"12439237654298374566\"]",{"VOID":1234},"Groves, M.L. (1960) The isolation of a red protein from milk2. J. Am. Chem. Soc. 82: 3345–3350.\nRoberts, A. K., R. Chierici, G. Sawatzki, M. J. Hill, S. Volpato, and V. Vigi (1992) Supplementation of an adapted formula with bovine lactoferrin: 1. Effect on the infant faecal flora. Acta Paediatr. 81: 119–124.\nJenssen, H. and R. E. Hancock (2009) Antimicrobial properties of lactoferrin. Biochimie. 91: 19–29.\nBellamy, W., M. Takase, K. Yamauchi, H. Wakabayashi, K. Kawase, and M. Tomita (1992) Identification of the bactericidal domain of lactoferrin. Biochim. Biophys. Acta. 1121: 130–136.\nArias, M., L. J. McDonald, E. F. Haney, K. Nazmi, J. G. Bolscher, and H. J. Vogel (2014) Bovine and human lactoferricin peptides: chimeras and new cyclic analogs. Biometals. 27: 935–948.\nGarcía-Montoya, I., S. A. González-Chávez, J. Salazar-Martínez, S. Arévalo-Gallegos, S. Sinagawa-García, and Q. Rascón-Cruz (2013) Expression and characterization of recombinant bovine lactoferrin in E. coli. Biometals. 26: 113–122.\nRosano, G. L. and E. A. Ceccarelli (2014) Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol. 5: 172.\nWang, S. H., T. S. Yang, S. M. Lin, M. S. Tsai, S. C. Wu, and S. J. Mao (2002) Expression, characterization, and purification of recombinant porcine lactoferrin in Pichia pastoris. Protein Expr. Purif. 25: 41–49.\nParamasivam, M., K. Saravanan, K. Urna, S. Sharma, T. P. Singh, and A. Srinivasan (2002) Expression, purification, and characterization of equine lactoferrin in Pichia pastoris. Protein Expr. Purif. 26: 28–34.\nDong, Z. Y. and Y. Z. Zhang (2006) Molecular cloning and expression of yak (Bos grunniens) lactoferrin cDNA in Pichia pastoris. Biotechnol. Lett. 28: 1285–1292.\nChen, G. H., L. J. Yin, I. H. Chiang, and S. T. Jiang (2007) Expression and purification of goat lactoferrin from Pichia pastoris expression system. J. Food. Sci. 72: M67–M71.\nIglesias-Figueroa, B., N. Valdiviezo-Godina, T. Siqueiros-Cendon, S. Sinagawa-García, S. Arévalo-Gallegos, and Q. Rascón-Cruz (2016) High-level expression of recombinant bovine lactoferrin in Pichia pastoris with antimicrobial activity. Int. J. Mol. Sci. 17: 902.\nSun, J., J. Jiang, L. Liu, Z. Wang, and C. Wei (2019) Expression of the hybrid antimicrobial peptide lactoferrin-lysozyme in Pichia pastoris. Biotechnol. Appl. Biochem. 66: 202–208.\nCudna, R. E. and A. J. Dickson (2003) Endoplasmic reticulum signaling as a determinant of recombinant protein expression. Biotechnol. Bioeng. 81: 56–65.\nDamasceno, L. M., C. J. Huang, and C. A. Batt (2012) Protein secretion in Pichia pastoris and advances in protein production. Appl. Microbiol. Biot. 93: 31–39.\nGuerfal, M., S. Ryckaert, P. P. Jacobs, P. Ameloot, K. Van Craenenbroeck, R. Derycke, and N. Callewaert (2010) The HAC1 gene from Pichia pastoris: characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins. Microb. Cell Fad. 9: 49.\nKim, M. D., K. C. Han, H. A. Kang, S. K. Rhee, and J. H. Seo (2003) Coexpression of BiP increased antithrombotic hirudin production in recombinant Saccharomyces cerevisiae. J. Biotechnol. 101: 81–87.\nShusta, E. V., R. T. Raines, A. Pluckthun, and K. D. Wittrup (1998) Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nat. Biotechnol. 16: 773–777.\nXu, N., J. Zhu, Q. Zhu, Y. Xing, M. Cai, T. Jiang, M. Zhou, and Y. Zhang (2018) Identification and characterization of novei promoters for recombinant protein production in yeast Pichia pastoris. Yeast. 35: 379–385.\nWessel, D. and U. I. Flilgge (1984) A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138: 141–143.\nLivak, K. J. and T. D. Schmittgen (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2-AACT method. Methods. 25: 402–408.\nTian, J., S. Shen, C. Zhou, X. Dang, Y. Jiao, L. Li, S. Ding, and H. Li (2015) Investigation of the antimicrobial activity and biocompatibility of magnesium alloy coated with HA and antimicrobial peptide. J. Mater Sci. Mater Med. 26: 66.\nSzymczak, A. L., C. J. Workman, Y. Wang, K. M. Vignali, S. Dilioglou, E. F. Vanin, and D. A. Vignali (2004) Correction of multi-gene deficiency in vivo using a single‘self-cleaving’2A peptide-based retroviral vector. Nat. Biotechnol. 22: 589–594.\nTang, X. S., Z. R. Tang, S. P. Wang, Z. M. Feng, D. Zhou, T. J. Li, and Y. L. Yin (2012) Expression, purification, and antibacterial activity of bovine lactoferrampin-lactoferricin in Pichia pastoris. Appl. Biochem. Biotechnol. 166: 640–651.\nChatterjee, M., C. P. Anju, L. Biswas, V. A. Kumar, C. G. Mohan, and R. Biswas (2016) Antibiotic resistance in Pseudomonas aeruginosa and alternative therapeutic options. Int. J. Med. Microbiol. 306: 48–58.\nChen, K., L. Chai, H. Li, Y. Zhang, H. M. Xie, J. Shang, W. Tian, P. Yang, and A. C. Jiang (2016) Effect of bovine lactoferrin from iron-fortified formulas on diarrhea and respiratory tract infections of weaned infants in a randomized controlled trial. Nutrition. 32: 222–227.\nManzoni, P., M. Meyer, I. Stolfi, M. Rinaldi, S. Cattani, L. Pugni, M. G. Romeo, H. Messner, L. Decembrino, N. Laforgia, R. Vagnarelli, L. Memo, L. Bordignon, M. Maule, E. Gallo, M. Mostert, M. Quercia, L. Bollanii, R. Pedicino, L. Renzullo, R. Betta, R. Ferrari, T. Alexander, R. Magaldi, D. Farina, R. Mosca, and M. Stronati (2014) Bovine lactoferrin supplementation for prevention of necrotizing enterocolitis in very-low-birth-weight neonates: a randomized clinical trial. Early Hum. Dev. 90: S60–S65.\nWeis, R., R. Luiten, W. Skranc, H. Schwab, M. Wubbolts, and A. Glieder (2004) Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena. FEMS Yeast Res. 5: 179–189.\nVogi, T., G. G. Thallinger, G. Zellnig, D. Drew, J. M. Cregg, A. Glieder, and M. Freigassner (2014) Towards improved membrane protein production in Pichia pastoris: general and specific transcriptional response to membrane protein overexpression. N. Biotechnol. 31: 538–552.\nFuller, R. S., R. E. Sterne, and J. Thorner (1988) Enzymes required for yeast prohormone processing. Annu. Rev. Physiol. 50: 345–362.\nRockwell, N. C., D. J. Krysan, T. Komiyama, and R. S. Fuller (2002) Precursor processing by kex2\u002Ffurin proteases. Chem. Rev. 102: 4525–4548.\nRockwell, N. C. and J. W. Thorner (2004) The kindest cuts of all: crystal structures of Kex2 and furin reveal secrets of precursor processing. Trends Biochem. Sci. 29: 80–87.\nYang, S., Y. Kuang, H. Li, Y. Liu, X. Hui, P. Li, Z. Jiang, Y. Zhou, Y. Wang, A. Xu, S. Li, P. Liu, and D. Wu (2013) Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1′site. PLoS One. 8: e75347.\nSchroder, M., R. Clark, and R. I. Kaufman (2003) IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast. Mol. Microbiol. 49: 591–606.\nFoti, D. M., A. Welihinda, R. J. Kaufman, and A. S. Lee (1999) Conservation and divergence of the yeast and mammalian unfolded protein response. Activation of specific mammalian endoplasmic reticulum stress element of the grp78\u002FBiP promoter by yeast Hacl. J. Biol. Chem. 274: 30402–30409.\nLin, X. Q., S. L. Liang, S. Y. Han, S. P. Zheng, Y. R. Ye, and Y. Lin (2013) Quantitative iTRAQ LC-MS\u002FMS proteomics reveals the cellular response to heterologous protein overexpression and the regulation of HAC1 in Pichia pastoris. J. Proteomics. 91: 58–72.\nBoettner, M., C. Steffens, C. von Mering, P. Bork, U. Stahl, and C. Lang (2007) Sequence-based factors influencing the expression of heterologous genes in the yeast Pichia pastoris—A comparative view on 79 human genes. J Biotechnol. 130: 1–10.\nRazaghi, A., E. Tan, L. H. L. Lua, L. Owens, O. P. Karthikeyan, and K. Heimann (2017) Is Pichia pastoris a realistic platform for industrial production of recombinant human interferon gamma? 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this study, we have described a method for the fabrication of a protein chip on silicon substrate using hydrophobic thin film and microfluidic channels, for the simultaneous detection of multiple targets in samples. The use of hydrophobic thin film provides for a physical, chemical, and biological barrier for protein patterning. The microfluidic channels create four protein patterned strips on the silicon surfaces with a high signal-to-noise ratio. The feasibility of the protein chips was determined in order to discriminate between each protein interaction in a mixture sample that included biotin, ovalbumin, hepatitis B antigen. In the fabrication of the multiplexed assay system, the utilization of the hydrophobic thin film and the microfluidic networks constitutes a more convenient method for the development of biosensors or biochips. This technique may be applicable to the simultaneous evaluation of multiple protein-protein interactions.",{"EN":1421},"Fabrication of disposable protein chip for simultaneous sample detection",{"VOID":1423},"[\"11972633780662673812\"]",{"VOID":1425},"Borrebaeck, C. A. (2006) Antibody microarray-based oncoproteomics.Expert Opin. Biol. Ther. 6: 833–838.\nBulyk, M. L. (2006) DNA microarray technologies for measuring protein-DNA interactions.Curr. Opin. Biotechnol. 17: 422–430.\nKim, C. G., J. J. Lee, D. Y. Jung, J. Jeon, H. S. Heo, H. C. Kang, J. H. Shin, Y. S. Cho, K. J. Cha, C. G. Kim, B. R. Do, K. S. Kim, and H. S. Kim (2006) Profilling of differentially expressed genes in human stem cells by cDNa microarray.Mol. Cells 21: 343–355.\nSato, K., A. Egami, T. Odake, M. Tokeshi, M. Aihara, and T. Kitamori (2006) Monitoring of intercellular messengers released from neuron networks cultured in a microchip.J. Chromatogr. A 1111: 228–252.\nLee, C. S., S. H. Lee, S. S. Park, Y. K. Kim, and B. G. Kim (2003) Protein patterning on silicon-based surface using background hydrophobic thin film.Biosens. Bioelectron. 18: 437–444.\nLee, C. S., S. H. Lee, Y. G. Kim. J. H. Lee, Y. K. Kim, and B. G. Kim (2006) A method of binding kinetics of a ligand to micropatterned proteins on a microfluidic chip.biosens. Bioelectron. In press.\nLee, S. H., C. S. Lee, D. S. Shin, B. G. Kim, Y. S. Lee, and Y. K. Kim (2004) Micro protein patterning using a lift-off process with fluorocarbon thin film.Sens. Actuators B Chem. 99: 623–632.\nBentzen, E. L., I. D. Tomlinson, J. Mason, P. Gresch, M. R. Warnement, D. Wright, E. Sanders-Bush, R. Blakely, and S. J. Rosenthal (2005) Surface modification to reduce nonspecific binding of quantum dots in live cell assays.Bioconjug. Chem. 16: 1488–1494.\nCha, T., A. Guo, Y. Jun, D. Pei, and X. Y. Zhu (2004) Immobilization of oriented protein molecules on poly (ethylene glycol)-coated Si(111).Proteomics 4: 1965–1976.\nPreininger, C., U. Sauer, W. Kern, and J. Dayteg (2004) Photoactivatable copolymers of vinylbenzyl thiocyanate as immobilization matrix for biochips.Anal. Chem. 76: 6130–6136.\nSchmalenberg, K. E., H. M. Buettner, and K. E. Uhrich (2004) Microcontact printing of proteins on oxygen plasma-activated poly(methyl methacrylate).Biomaterials 25: 1851–1857.\nWilkop, T., Z. Wang, and Q. Cheng (2004) Analysis of micro-contact printed protein patterns by SPR imaging with a LED light source.Langmuir 20: 11141–11148.\nLee, C. S. and B. G. Kim (2002) Improvement of protein stability in protein microarrays.Biotechnol. Lett. 24: 839–844.\nLee, C. S., S. H. Lee, Y. G. Kim, C. H. Choi., Y. K. Kim, and B. G. Kim (2006) Biochemical reactions on a micro-fluidic chip based on a precise fluidic handling method at the nanoliter scale.Biotechnol. Bioprocess. Eng. 11: 146–153.\nPark, S. S., H. S. Joo, S. I. Cho, M. S. Kim, Y. K. Kim, and B. G. Kim (2003) Multi-step reactions on microchip platform using nitrocellulose membrane reactor.Biotechnol. Bioprocess Eng. 8: 257–262.\nHui, A. Y., G. Wang, B. Lin, and W. T. Chan (2005) Microwave plasma treatment of polymer surface for irreversible sealing of micro fluidic devices.Lab Chip 5: 1173–1177.\nMarquette, C. A. and L. J. Blum (2006) State of the art and recent advances in immunoanalytical systems.Biosens. Bioelectron. 21: 1424–1433.\nDupuy, A. M., S. Lehmann, and J. P. Cristol (2005) Protein biochip systems for the clinical laboratory.Clin. Chem. Lab. Med. 43: 1291–1302.\nRichalet-Secordel, P. M., F. Poisson, and M. H. Van Regenmortel (1996) Uses of biosensor technology in the development of probes for viral diagnosis.Clin. Diagn. Virol. 5: 111–119.\nPurvis, D., O. Leonardova, D. Farmakovsky, and V. Cherkasov (2003) An ultrasensitive and stable potentiometric immunosensor.Biosens. Bioelectron. 18: 1385–1390.\nLee, W. E., H. G. Thompson, J. G. Hall, and D. E. Bader (2000) Rapid detection and identification of biological and chemical agents by immunoassay, gene probe assay and enzyme inhibition using a silicon-based biosensor.Biosens. Bioelectron. 14: 795–804.\nChoi, W. J. and J. K. Park (2006) A bio-fluiclic device for adaptive sample pretreatment and its application to measurements ofEscherichia coli concentrations.Biotechnol. Bioprocess Eng. 11: 54–60.\nChoi, J. W., Y. S. Nam, and M. Fujihira (2004) Nanoscale fabrication of biomolecular layer and its application to biodevices.Biotechnol. 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(NIR) irradiation-responsive drug carriers are of great interest because the light is tissue-penetrating and the carriers administered into human body can be made to release their payloads at a specific site in an active manner using the external stimulus (i.e., NIR irradiation). In this study, thermo-responsive liposomes bearing gold nanoparticle (GNP) were developed as a NIR irradiation-responsive drug carrier. Dipalmitoylphosphatidyl-choline (DPPC) liposome was surface-decorated with hydrophobically modified thiolated carboxymethyl cellulose (Hm TL-CMC)-capped GNP and hydrophobically modified poly(N-isopropylacrylamide) (Hm PNIPAM). GNP was prepared using Hm TL-CMC as a reducing agent for gold ions and a capping material for GNP. DPPC liposomes incorporating Hm TL-CMC-capped GNP and Hm PNIPAM were prepared by a film hydration and sonication method and they exhibited a multi lamellar structure along with GNP on its transmission electron micrograph. The temperature-responsive release of DPPC liposome was promoted when the liposome was incorporating Hm PNIPAM, possibly due to the thermal contraction of the polymer chains. DPPC liposome incorporating Hm TL-CMC-capped GNP showed a NIR-responsive release, possibly due to the photothermal effect of GNP, and the NIR-responsive release was enhanced when the liposome was bearing Hm PNIPAM.",{"EN":1655},"Near-infrared and Thermo-sensitive Liposomes Incorporating Thiolated-carboxymethyl Cellulose-capped Gold Nanoparticles and Poly(N-isopropylacrylamide)",{"VOID":1657},"[\"2896447719941366228\"]",{"VOID":1659},"Tan, S., T. Wu, D. Zhang, and Z. Zhang (2015) Cell or cell membrane-based drug delivery systems. Theranostics 5: 863–881.\nFazal, S., and R. Lee (2021) Biomimetic bacterial membrane vesicles for drug delivery applications. Pharmaceutics 13: 1430.\nHammoud, Z., N. Khreich, L. Auezova, S. Fourmentin, A. Elaissari, and H. Greige-Gerges (2019) Cyclodextrin-membrane interaction in drug delivery and membrane structure maintenance. Int. J. Pharm. 564: 59–76.\nCevc, G. (2004) Lipid vesicles and other colloids as drug carriers on the skin. Adv. Drug Deliv. Rev. 56: 675–711.\nPignatello, R., T. Musumeci, L. Basile, C. Carbone, and G. Puglisi (2011) Biomembrane models and drug-biomembrane interaction studies: involvement in drug design and development. J. Pharm. Bioallied Sci. 3: 4–14.\nLi, D., X. An, and Y. Mu (2019) A liposomal hydrogel with enzyme triggered release for infected wound. Chem. Phys. Lipids 223: 104783.\nNemoto, R., K. Fujieda, Y. Hiruta, M. Hishida, E. Ayano, Y. Maitani, K. Nagase, and H. Kanazawa (2019) Liposomes with temperature-responsive reversible surface properties. Colloids Surf. B Biointerfaces 176: 309–316.\nRefaat, A., B. Del Rosal, J. Palasubramaniam, G. Pietersz, X. Wang, S. E. Moulton, and K. Peter (2021) Near-infrared light-responsive liposomes for protein delivery: towards bleeding-free photothermally-assisted thrombolysis. J. Control. Release 337: 212–223.\nObata, Y., S. Tajima, and S. Takeoka (2010) Evaluation of pH-responsive liposomes containing amino acid-based zwitterionic lipids for improving intracellular drug delivery in vitro and in vivo. J. Control. Release 142: 267–276.\nRaza, A., U. Hayat, T. Rasheed, M. Bilal, and H. M. N. Iqbal (2018) Redox-responsive nano-carriers as tumor-targeted drug delivery systems. Eur. J. Med. Chem. 157: 705–715.\nNappini, S., S. Fogli, B. Castroflorio, M. Bonini, F. B. Bombelli, and P. Baglioni (2016) Magnetic field responsive drug release from magnetoliposomes in biological fluids. J. Mater. Chem. B 4: 716–725.\nKim, J. A., and J.-C. Kim (2018) Temperature and electric field-triggerable liposomes incorporating poly(hydroxyethyl acrylate-co-hexadecyl acrylate-co-carboxyethyl acrylate). J. Ind. Eng. Chem. 62: 383–391.\nHayashi, H., K. Kono, and T. Takagishi (1996) Temperature-controlled release property of phospholipid vesicles bearing a thermo-sensitive polymer. Biochim. Biophys. Acta 1280: 127–134.\nTa, T., and T. M. Porter (2013) Thermosensitive liposomes for localized delivery and triggered release of chemotherapy. J. Control. Release 169: 112–125.\nKneidl, B., M. Peller, G. Winter, L. H. Lindner, and M. Hossann (2014) Thermosensitive liposomal drug delivery systems: state of the art review. Int. J. Nanomedicine 9: 4387–4398.\nPapahadjopoulos, D., K. Jacobson, S. Nir, and I. Isac (1973) Phase transitions in phospholipid vesicles. Fluorescence polarization and permeability measurements concerning the effect of temperature and cholesterol. Biochim. Biophys. Acta 311: 330–348.\nGarcia-Manyes, S., G. Oncins, and F. Sanz (2005) Effect of temperature on the nanomechanics of lipid bilayers studied by force spectroscopy. Biophys. J. 89: 4261–4274.\nKim, J.-C., S. K. Bae, and J. D. Kim (1997) Temperature-sensitivity of liposomal lipid bilayers mixed with poly(N-isopropylacrylamide-co-acrylic acid). J. Biochem. 121: 15–19.\nGuo, H., and J.-C. Kim (2015) Photothermally induced release from liposome suspended in mixture solution of gold nanoparticle and thermo-sensitive polymer. Colloids Surf. A Physicochem. Eng. Asp. 469: 73–82.\nEskandari, P., H. Roghani-Mamaqani, M. Salami-Kalajahi, and Z. Abousalman-Rezvani (2020) Modification of cellulose nanocrystal with dual temperature- and CO2-responsive block copolymers for ion adsorption applications. J. Mol. Liq. 310: 113234.\nCummings, C., H. Murata, R. Koepsel, and A. J. Russell (2013) Tailoring enzyme activity and stability using polymer-based protein engineering. Biomaterials 34: 7437–7443.\nMohapatra, S. S., S. Ranjan, N. Dasgupta, R. Kumar Mishra, and S. Thomas (2018) Applications of Targeted Nanodrugs and Delivery Systems: Nanoscience and Nanotechnology in Drug Delivery. pp. 133–155. Elsevier.\nLanzalaco, S., and E. Armelin (2017) Poly(N-isopropylacrylamide) and copolymers: a review on recent progresses in biomedical applications. Gels 3: 36.\nMai, B. T., S. Fernandes, P. B. Balakrishnan, and T. Pellegrino (2018) Nanosystems based on magnetic nanoparticles and thermo- or pH-responsive polymers: an update and future perspectives. Acc. Chem. Res. 51: 999–1013.\nWang, M., and J.-C. Kim (2014) Light- and temperature-responsive liposomes incorporating cinnamoyl Pluronic F127. Int. J. Pharm. 468: 243–249.\nZhang, H., and J.-C. Kim (2015) Hydroxyethyl acrylate-based polymeric amphiphiles showing lower critical solution temperature. J. Macromol. Sci. Part A 52: 138–146.\nSteinhauer, W., R. Hoogenboom, H. Keul, and M. Moeller (2010) Copolymerization of 2-hydroxyethyl acrylate and 2-methoxyethyl acrylate via RAFT: kinetics and thermoresponsive properties. Macromolecules 43: 7041–7047.\nMathiyazhakan, M., C. Wiraja, and C. Xu (2018) A concise review of gold nanoparticles-based photo-responsive liposomes for controlled drug delivery. Nanomicro Lett. 10: 10.\nJain, K., R. Vedarajan, M. Watanabe, M. Ishikiriyama, and N. Matsumi (2015) Tunable LCST behavior of poly(N-isopropylacrylamide\u002Fionic liquid) copolymers. Polym. Chem. 6: 6819–6825.\nGandhi, A., A. Paul, S. O. Sen, and K. K. Sen (2015) Studies on thermoresponsive polymers: phase behaviour, drug delivery and biomedical applications. Asian J. Pharm. Sci. 10: 99–107.\nBokias, G., G. Staikos, and I. Iliopoulos (2000) Solution properties and phase behaviour of copolymers of acrylic acid with N-isopropylacrylamide: the importance of the intrachain hydrogen bonding. Polymer (Guildf.) 41: 7399–7405.\nXie, R., Y. Li, and L.-Y. Chu (2007) Preparation of thermo-responsive gating membranes with controllable response temperature. J. Memb. Sci. 289: 76–85.\nChung, J. E., M. Yokoyama, T. Aoyagi, Y. Sakurai, and T. Okano (1998) Effect of molecular architecture of hydrophobically modified poly(N-isopropylacrylamide) on the formation of thermoresponsive core-shell micellar drug carriers. J. Control. Release 53: 119–130.\nLiu, R., M. Fraylich, and B. R. Saunders (2009) Thermoresponsive copolymers: from fundamental studies to applications. Colloid Polym. Sci. 287: 627–643.\nNagy-Simon, T., M. Potara, A. M. Craciun, E. Licarete, and S. Astilean (2018) IR780-dye loaded gold nanoparticles as new near infrared activatable nanotheranostic agents for simultaneous photodynamic and photothermal therapy and intracellular tracking by surface enhanced resonant Raman scattering imaging. J. Colloid Interface Sci. 517: 239–250.\nWang, H., W. Ouyang, X. Zhang, J. Xue, X. Lou, R. Fan, X. Zhao, L. Shan, and T. Jiang (2019) Bacteria-induced aggregation of bioorthogonal gold nanoparticles for SERS imaging and enhanced photothermal ablation of Gram-positive bacteria. J. Mater. Chem. B 7: 4630–4637.\nVines, J. B., J.-H. Yoon, N.-E. Ryu, D.-J. Lim, and H. Park (2019) Gold nanoparticles for photothermal cancer therapy. Front. Chem. 7: 167.\nAmendola, V., R. Pilot, M. Frasconi, O. M. Maragò, and M. A. Iatì (2017) Surface plasmon resonance in gold nanoparticles: a review. J. Phys. Condens. Matter 29: 203002.\nAl Mahrouqi, D., J. Vinogradov, and M. D. Jackson (2017) Zeta potential of artificial and natural calcite in aqueous solution. Adv. Colloid Interface Sci. 240: 60–76.\nYang, F., W. Wu, S. Chen, and W. Gan (2017) The ionic strength dependent zeta potential at the surface of hexadecane droplets in water and the corresponding interfacial adsorption of surfactants. Soft Matter 13: 638–646.\nMirhosseini, H., C. P. Tan, N. S. A. Hamid, and S. Yusof (2008) Effect of Arabic gum, xanthan gum and orange oil contents on ζ-potential, conductivity, stability, size index and pH of orange beverage emulsion. Colloids Surf. A Physicochem. Eng. Asp. 315: 47–56.\nSrinivasan, S., S. A. Barbhuiya, D. Charan, and S. P. Pandey (2010) Characterising cement-superplasticiser interaction using zeta potential measurements. Constr. Build. Mater. 24: 2517–2521.\nElbasuney, S. (2017) Sustainable steric stabilization of colloidal titania nanoparticles. Appl. Surf. Sci. 409: 438–447.\nBadley, R. D., W. T. Ford, F. J. McEnroe, and R. A. Assink (1990) Surface modification of colloidal silica. Langmuir 6: 792–801.\nKorkmaz, F., and F. Severcan (2005) Effect of progesterone on DPPC membrane: evidence for lateral phase separation and inverse action in lipid dynamics. Arch. Biochem. Biophys. 440: 141–147.\nJing, Y., H. Trefna, M. Persson, B. Kasemo, and S. Svedhem (2014) Formation of supported lipid bilayers on silica: relation to lipid phase transition temperature and liposome size. Soft Matter 10: 187–195.",{"VOID":1661},"10.1007\u002Fs12257-022-0378-0","2024-08-31T01:15:40.341+00:00","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs12257-022-0378-0",[1665,1680,1693],{"id":1666,"sortIndex":21,"researcher":20,"roles":1667,"affiliations":1668,"properties":1677,"displayName":1679,"givenName":20,"familyName":20},"251156ca-5c8b-4d7f-a4e9-cac73b2e4b33",[229],[1669],{"id":1670,"sortIndex":21,"affiliation":1671,"properties":20},"f148742e-5234-41a7-842e-bdc55ab18a00",{"id":1670,"createTime":20,"updateTime":20,"relativeEntities":1672,"slug":20,"properties":1673,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1676,"statistic":20},[],{"title":1674},{"VI":1675},"Department of Biomedical Science & Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon, Korea",[],{"title":1678},{"VI":1679},"Fanyu 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yeasts are promising cell factories to produce lipids and oleochemicals, metabolites of industrial interest (e.g., organics acids, esters, and alcohols), and enzymes. They can also use different agro-industrial by-products as substrates within the context of a circular economy. Some of these yeasts can also comprise economic and health burdens as pathogens. Genome-scale metabolic models (GEMs), networks reconstructed based on the genomic and metabolic information of one or more organisms, are great tools to understand metabolic functions and landscapes, as well as propose engineering targets to improve metabolite production or propose novel drug targets. Previous reviews on yeast GEMs have mainly focused on the history and the evaluation of Saccharomyces cerevisiae modeling paradigms or the accessibility and usability of yeast GEMs. However, they did not describe the reconstruction strategies, limitations, validations, challenges, and research gaps of non-conventional yeast GEMs. Herein, we focused on the reconstruction of available non-Saccharomyces GEMs, their validation, underscoring the physiological insights, as well as the identification of both metabolic engineering and drug targets. We also discuss the challenges and knowledge gaps and propose strategies to boost their use and novel reconstructions.",{"EN":1782},"Reconstruction of genome-scale metabolic models of non-conventional yeasts: current state, challenges, and perspectives",{"VOID":1784},"[\"4104249937115062159\"]",{"VOID":1786},"Boekhout T, Amend A, El Baidouri F et al (2022) Trends in yeast diversity discovery. 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Catalysts 11:1291\nPham N, Reijnders M, Suarez-Diez M et al (2021) Genome-scale metabolic modeling underscores the potential of Cutaneotrichosporon oleaginosus ATCC 20509 as a cell factory for biofuel production. Biotechnol Biofuels 14:2. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs13068-020-01838-1\nde Almeida ELM, Ventorim RZ, de Moura Ferreira MA et al (2022) Papiliotrema laurentii: general features and biotechnological applications. Appl Microbiol Biotechnol 106:6963–6976. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00253-022-12208-2\nVentorim RZ, de Moura Ferreira MA, de Almeida ELM et al (2022) Genome-scale metabolic model of oleaginous yeast Papiliotrema laurentii. Biochem Eng J 180:108353\nSegrè D, Vitkup D, Church GM (2002) Analysis of optimality in natural and perturbed metabolic networks. Proc Natl Acad Sci U S A 99:15112–15117. https:\u002F\u002Fdoi.org\u002F10.1073\u002Fpnas.232349399\nKim M, Park BG, Kim EJ et al (2019) In silico identification of metabolic engineering strategies for improved lipid production in Yarrowia lipolytica by genome-scale metabolic modeling. Biotechnol Biofuels 12:187. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs13068-019-1518-4\nOlicón-Hernández DR, Araiza-Villanueva MG, Pardo JP et al (2019) New insights of Ustilago maydis as yeast model for genetic and biotechnological research: a review. Curr Microbiol 76:917–926. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00284-019-01629-4\nKarp PD, Midford PE, Billington R et al (2021) Pathway Tools version 23.0 update: software for pathway\u002Fgenome informatics and systems biology. Brief Bioinform 22:109–126. https:\u002F\u002Fdoi.org\u002F10.1093\u002Fbib\u002Fbbz104\nSrikanta D, Santiago-Tirado FH, Doering TL (2014) Cryptococcus neoformans: historical curiosity to modern pathogen. Yeast 31:47–60. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fyea.2997\nRathore SS, Sathiyamoorthy J, Lalitha C et al (2022) A holistic review on Cryptococcus neoformans. Microb Pathog 166:105521. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.micpath.2022.105521\nHenson MA, Orazi G, Phalak P et al (2019) Metabolic modeling of cystic fibrosis airway communities predicts mechanisms of pathogen dominance. mSystems 4:e00026-19. https:\u002F\u002Fdoi.org\u002F10.1128\u002FmSystems.00026-19\nPitkänen E, Jouhten P, Hou J et al (2014) Comparative genome-scale reconstruction of gapless metabolic networks for present and ancestral species. PLoS Comput Biol 10:e1003465. https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pcbi.1003465\nCorreia K, Mahadevan R (2020) Pan-genome-scale network reconstruction: harnessing phylogenomics increases the quantity and quality of metabolic models. Biotechnol J 15:e1900519. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fbiot.201900519\nLu H, Li F, Yuan L et al (2021) Yeast metabolic innovations emerged via expanded metabolic network and gene positive selection. Mol Syst Biol 17:e10427. https:\u002F\u002Fdoi.org\u002F10.15252\u002Fmsb.202110427\nLu H, Kerkhoven EJ, Nielsen J (2022) A pan-draft metabolic model reflects evolutionary diversity across 332 yeast species. Biomolecules 12:1632. https:\u002F\u002Fdoi.org\u002F10.3390\u002Fbiom12111632\nShen XX, Opulente DA, Kominek J et al (2018) Tempo and mode of genome evolution in the budding yeast subphylum. Cell 175:1533-1545.e20. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cell.2018.10.023\nDomenzain I, Sánchez B, Anton M et al (2022) Reconstruction of a catalogue of genome-scale metabolic models with enzymatic constraints using GECKO 2.0. Nat Commun 13:3766. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41467-022-31421-1",{"VOID":1788},"10.1007\u002Fs12257-024-00009-5","2024-06-24T23:30:28.902+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12257-024-00009-5",[1792,1809,1834],{"id":1793,"sortIndex":21,"researcher":20,"roles":1794,"affiliations":1795,"properties":1804,"displayName":1806,"givenName":20,"familyName":20},"1d60c5d9-b239-4a06-99a7-8c235db7d2ac",[229],[1796],{"id":1797,"sortIndex":21,"affiliation":1798,"properties":20},"3d291419-8a2d-4099-90f8-ad8cf25ca2e3",{"id":1797,"createTime":20,"updateTime":20,"relativeEntities":1799,"slug":20,"properties":1800,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1803,"statistic":20},[],{"title":1801},{"VI":1802},"Laboratory of Microbial Physiology, Department of Microbiology, Universidade Federal de Viçosa, Viçosa, Brazil",[],{"title":1805,"gsAuthor":1807},{"VI":1806},"Eduardo Luís Menezes de Almeida",{"VOID":1808},"[\"hdfB-ogAAAAJ\"]",{"id":1810,"sortIndex":172,"researcher":20,"roles":1811,"affiliations":1812,"properties":1829,"displayName":1831,"givenName":20,"familyName":20},"e9dfe8ea-7b5c-49fc-9edf-78c44adc46e1",[229],[1813,1821],{"id":1814,"sortIndex":21,"affiliation":1815,"properties":20},"181f078f-c0d0-4bc9-b0a1-76c480c2bcb5",{"id":1814,"createTime":20,"updateTime":20,"relativeEntities":1816,"slug":20,"properties":1817,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1820,"statistic":20},[],{"title":1818},{"VI":1819},"Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden",[],{"id":1822,"sortIndex":172,"affiliation":1823,"properties":20},"18863e30-4cdf-4ef6-987d-0c55cf53a17b",{"id":1822,"createTime":20,"updateTime":20,"relativeEntities":1824,"slug":20,"properties":1825,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1828,"statistic":20},[],{"title":1826},{"VI":1827},"SciLifeLab, Chalmers University of Technology, Gothenburg, Sweden",[],{"title":1830,"gsAuthor":1832},{"VI":1831},"Eduard J. 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inflammatory response is an indispensable bodily reaction, but excessive inflammation is known to result in diseases such as atopic disease, bronchitis, rheumatoid arthritis, and inflammatory bowel disease. Ceramide is the basic structure of sphingolipids and ceramides have been industrially used in functional cosmetics as anti-aging agents, as well as for moisturizing skin and calming skin irritation. It also has been recently used in medicinal fields as an anti-inflammatory as well as for atopic and skin wound healing, and for skin barrier restoration. In this study, we used genetically modified Saccharomyces cerevisiae to produce ceramides. Ceramide mixture was produced by gene manipulation that amplifies the original yeast gene. To investigate their anti-inflammatory effects, nitric oxide (NO) concentrations in cell culture supernatant were measured by using the Griess reaction and the expression levels of pro-inflammatory markers, cyclooxygenase-2 (COX-2) and tumor necrosis factor-α (TNF-α), were determined by using qRT-PCR. When cells were treated with the ceramide mixture, cell viability was not reduced, but NO production was inhibited. In addition, expressions of COX-2 and TNF-α were inhibited. Based on these results, we conclude that ceramide biosynthesized from recombinant yeast can effectively reduce the expression of inflammatory enzymes and cytokines. We expected that ceramides biosynthesized in genetically modified yeast is a novel preventive or therapeutic agent for inflammatory diseases without the risk of foreign gene introduction.",{"EN":1922},"Anti-inflammatory effect of the ceramide mixture extracted from genetically modified Saccharomyces cerevisiae",{"VOID":1924},"[\"7904062662373494198\"]",{"VOID":1926},"Coderch, L., O. López, A. De La Maza, and J. L. Parra (2003) Ceramides and skin function. Am. J. Clin. Dermatol. 4: 107–129.\nRupčić, J., M. Mesarić, and V. Marić (1998) The influence of carbon source on the level and composition of ceramides of the Candida lipolytica yeast. Appl. Microbiol. Biotechnol. 50: 583–588.\nKwun, K. H., J. H. Lee, K. H. Rho, and H. S. Yun (2006) Production of ceramide with Saccharomyces cerevisiae. Appl. Biochem. Biotechnol. 133: 203–210.\nDickson, R. C. and R. L. Lester (1999) Yeast sphingolipids. Biochim. Biophys. Acta 1426: 347–357.\nRupčić, J. and V. Marić (1998) Isolation and chemical composition of the ceramide of the Candida lipolytica yeast. Chem. Phys. Lipids 91: 153–161.\nBlaise, G. A., D. Gauvin, M. Gangal, and S. Authier (2005) Nitric oxide, cell signaling and cell death. Toxicol. 208: 177–192.\nAndrew, P. J. and B. Mayer (1999) Enzymatic function of nitric oxide synthases. Cardiovasc. Res. 43: 521–531.\nShin, J. S., S. J. Park, S. Ryu, H. B. Kang, T. W. Kim, J. H. Choi, J. Y. Lee, Y. W. Cho, and K. T. Lee (2012) Potent antiinflammatory effect of a novel furan-2,5-dione derivative, BPD, mediated by dual suppression of COX-2 activity and LPSinduced inflammatory gene expression via NF-kB inactivation. Br. J. Pharmacol. 165: 1926–1940.\nSimpson, E. L. (2010) Atopic dermatitis: A review of topical treatment options. Curr. Med. Res. Opin. 26: 633–640.\nKim, S. K., Y. H. Noh, J. R. Koo, N. A. Da Silva, and H. S. Yun (2011) Effects of expression of lcb1\u002Flcb2 and lac1\u002Flag1 genes on the biosynthesis of ceramides. Biotechnol. Bioproc. Eng. 16: 1–6.\nPark, G. M., J. G. Jun, and J. K. Kim (2013) XH-14, a novel danshen methoxybenzo[b]furan derivative, exhibits anti-inflammatory properties in lipopolysaccharide-treated RAW 264.7 cells. J. Inflamm. 10: 1.\nLivak, K. J. and T. D. Schmittgen (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method. Methods 25: 402–408.\nHsu, Y., K. Chi, W. Huang, and W. Lin (2001) Ceramide inhibits lipopolysaccharide-mediated nitric oxide synthase and cyclooxygenase-2 induction in macrophages: Effects on protein kinases and transcription factors. J. Immunol. 166: 5388–5397.\nLiang, Y. C., Y. T. Huang, S. H. Tsai, S. Y. Lin-Shiau, C. F. Chen, and J. K. Lin (1999) Suppression of inducible cyclooxygenase and inducible nitric oxide synthase by apigenin and related flavonoids in mouse macrophages. Carcinogen. 20: 1945–1952.\nChristiaens, I., D. B. Zaragoza, L. Guilbert, S. A. Robertson, B. F. Mitchell, and D. M. Olson (2008) Inflammatory processes in preterm and term parturition. J. Reprod. Immunol. 79: 50–57.\nKiemer, A. K., C. Müller, and A. M. Vollmar (2002) Inhibition of LPS-induced nitric oxide and TNF-α production by α -lipoic acid in rat Kupffer cells and in RAW 264. 7 murine macrophages. Immunol. Cell Biol. 80: 550–557.\nKwon, S. and S. C. George (1999) Synergistic cytokine-induced nitric oxide production in human alveolar epithelial cells. Nitric Oxide 3: 348–357.\nKamle, S. and S. Ali (2013) Genetically modified crops: Detection strategies and biosafety issues. Gene 522: 123–132.",{"VOID":1928},"10.1007\u002Fs12257-017-0216-y","2024-06-25T22:16:15.938+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12257-017-0216-y",[1932,1949,1964,1977],{"id":1933,"sortIndex":21,"researcher":20,"roles":1934,"affiliations":1935,"properties":1944,"displayName":1946,"givenName":20,"familyName":20},"6c1868b8-f8f2-482a-acf6-53bbf75214ad",[229],[1936],{"id":1937,"sortIndex":21,"affiliation":1938,"properties":20},"185f3369-d29a-460a-aee3-e39979f0ce60",{"id":1937,"createTime":20,"updateTime":20,"relativeEntities":1939,"slug":20,"properties":1940,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1943,"statistic":20},[],{"title":1941},{"VI":1942},"Department of Biological Engineering, Inha University, Incheon, Korea",[],{"title":1945,"gsAuthor":1947},{"VI":1946},"Myeongkwan 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