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Volumn 6, Issue 1, 2013, Pages

The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor

Author keywords

Acetylxylan esterase Acremonium alcalophilum; Heterologous expression; Lipase; Nicotiana benthamiana

Indexed keywords

ACREMONIUM; AMINO ACID SEQUENCE; CARBON-CHAIN LENGTH; CELLULOLYTIC FUNGUS; HETEROLOGOUS EXPRESSION; MEDIUM-CHAIN FATTY ACIDS; NICOTIANA BENTHAMIANA; TOTAL SOLUBLE PROTEIN;

EID: 84880912278     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-6-111     Document Type: Article
Times cited : (11)

References (43)
  • 2
    • 24944592023 scopus 로고    scopus 로고
    • Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11
    • DOI 10.1016/j.enzmictec.2005.06.003, PII S0141022905002292
    • Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11. Castro-Ochoa LD, Rodríguez-Gómez C, Valerio-Alfaro G, Oliart Ros R, Enzyme Micob Technol 2005 37 648 654 10.1016/j.enzmictec.2005.06.003 (Pubitemid 41306252)
    • (2005) Enzyme and Microbial Technology , vol.37 , Issue.6 , pp. 648-654
    • Castro-Ochoa, L.D.1    Rodriguez-Gomez, C.2    Valerio-Alfaro, G.3    Oliart Ros, R.4
  • 3
    • 81355161500 scopus 로고    scopus 로고
    • Expression and characterization of a novel lipase from Aspergillus fumigatus with high specific activity
    • 10.1007/s12010-011-9311-2 21744116
    • Expression and characterization of a novel lipase from Aspergillus fumigatus with high specific activity. Shangguan JJ, Liu YQ, Wang FJ, Zhao J, Fan LQ, Li SX, Xu JH, Appl Biochem Biotechnol 2011 165 949 962 10.1007/s12010-011-9311-2 21744116
    • (2011) Appl Biochem Biotechnol , vol.165 , pp. 949-962
    • Shangguan, J.J.1    Liu, Y.Q.2    Wang, F.J.3    Zhao, J.4    Fan, L.Q.5    Li, S.X.6    Xu, J.H.7
  • 4
    • 69549087925 scopus 로고    scopus 로고
    • Distinction between esterases and lipases: Comparative biochemical properties of sequence-related carboxylesterases
    • 10.2174/092986609789071333 19508178
    • Distinction between esterases and lipases: comparative biochemical properties of sequence-related carboxylesterases. Chahiniana H, Sarda L, Protein Pept Lett 2009 16 1149 1161 10.2174/092986609789071333 19508178
    • (2009) Protein Pept Lett , vol.16 , pp. 1149-1161
    • Chahiniana, H.1    Sarda, L.2
  • 5
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • DOI 10.1016/S0167-7799(98)01195-0, PII S0167779998011950
    • Microbial lipases form versatile tools for biotechnology. Jaeger K-E, Reetz MT, Trends Biotechnol 1998 16 396 403 10.1016/S0167-7799(98)01195-0 9744114 (Pubitemid 28410428)
    • (1998) Trends in Biotechnology , vol.16 , Issue.9 , pp. 396-403
    • Jaeger, K.-E.1    Reetz, M.T.2
  • 6
    • 84856245910 scopus 로고    scopus 로고
    • Overview of fungal lipase: A review
    • 10.1007/s12010-011-9444-3 22072143
    • Overview of fungal lipase: a review. Singh A, Mukhopadhyay M, Appl Biochem Biotechnol 2012 166 486 520 10.1007/s12010-011-9444-3 22072143
    • (2012) Appl Biochem Biotechnol , vol.166 , pp. 486-520
    • Singh, A.1    Mukhopadhyay, M.2
  • 7
    • 45149118776 scopus 로고    scopus 로고
    • Welcome to Biotechnology for Biofuels
    • DOI 10.1186/1754-6834-1-1
    • Implications of cellobiohydrolase glycosylation for use in biomass conversion. Jeoh T, Michener W, Himmel M, Decker S, Adney W, Biotechnol Biofuels 2008 1 1 12 10.1186/1754-6834-1-1 18471312 (Pubitemid 351827653)
    • (2008) Biotechnology for Biofuels , vol.1 , pp. 1
    • Hahn-Hagerdal, B.1    Himmel, M.E.2    Somerville, C.3    Wyman, C.4
  • 8
    • 78650036190 scopus 로고    scopus 로고
    • Green biofactories: Recombinant protein production in plants
    • 10.2174/187220810793611464 21171961
    • Green biofactories: recombinant protein production in plants. Ahmad A, Pereira EO, Conley AJ, Richman AS, Menassa R, Recent Pat Biotechnol 2010 4 242 259 10.2174/187220810793611464 21171961
    • (2010) Recent Pat Biotechnol , vol.4 , pp. 242-259
    • Ahmad, A.1    Pereira, E.O.2    Conley, A.J.3    Richman, A.S.4    Menassa, R.5
  • 10
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • DOI 10.1146/annurev.micro.53.1.315
    • Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Jaeger KE, Dijkstra BW, Reetz MT, Annu Rev Microbiol 1999 53 315 351 10.1146/annurev.micro.53.1.315 10547694 (Pubitemid 29503734)
    • (1999) Annual Review of Microbiology , vol.53 , pp. 315-351
    • Jaeger, K.-E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 11
    • 0026700544 scopus 로고
    • Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa PAO1
    • 10.1099/00221287-138-7-1325 1512563
    • Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa PAO1. Wohlfarth S, Hoesche C, Strunk C, Winkler UK, J Gen Microbiol 1992 138 1325 1335 10.1099/00221287-138-7-1325 1512563
    • (1992) J Gen Microbiol , vol.138 , pp. 1325-1335
    • Wohlfarth, S.1    Hoesche, C.2    Strunk, C.3    Winkler, U.K.4
  • 12
    • 0037124354 scopus 로고    scopus 로고
    • A viral protein suppresses RNA silencing and binds silencing-generated, 21- to 25-nucleotide double-stranded RNAs
    • DOI 10.1093/emboj/cdf312
    • A viral protein suppresses RNA silencing and binds silencing-generated, 21- to 25-nucleotide double-stranded RNAs. Silhavy D, Molnar A, Lucioli A, Szittya G, Hornyik C, Tavazza M, Burgyan J, EMBO J 2002 21 3070 3080 10.1093/emboj/cdf312 12065420 (Pubitemid 34670391)
    • (2002) EMBO Journal , vol.21 , Issue.12 , pp. 3070-3080
    • Silhavy, D.1    Molnar, A.2    Lucioli, A.3    Szittya, G.4    Hornyik, C.5    Tavazza, M.6    Burgyan, J.7
  • 13
    • 0033748096 scopus 로고    scopus 로고
    • Purification, properties, and molecular cloning of a novel Ca(2+)-binding protein in radish vacuoles
    • 10.1104/pp.124.3.1069 11080284
    • Purification, properties, and molecular cloning of a novel Ca(2+)-binding protein in radish vacuoles. Yuasa K, Maeshima M, Plant Physiol 2000 124 1069 1078 10.1104/pp.124.3.1069 11080284
    • (2000) Plant Physiol , vol.124 , pp. 1069-1078
    • Yuasa, K.1    Maeshima, M.2
  • 14
    • 84902212491 scopus 로고    scopus 로고
    • In Planta Production of Cell Wall Degrading Enzymes
    • Boca Raton, FL: CRC Press Kole C, Joshi CP, Shonnard DR
    • In Planta Production of Cell Wall Degrading Enzymes. Karen AM, Handbook of Bioenergy Crop Plants Boca Raton, FL: CRC Press, Kole C, Joshi CP, Shonnard DR, 2012 55 73
    • (2012) Handbook of Bioenergy Crop Plants , pp. 55-73
    • Karen, A.M.1
  • 15
    • 0031613603 scopus 로고    scopus 로고
    • Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1
    • 10.1271/bbb.62.66 9501519
    • Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1. Kim HK, Park SY, Lee JK, Oh TK, Biosci Biotechnol Biochem 1998 62 66 71 10.1271/bbb.62.66 9501519
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 66-71
    • Kim, H.K.1    Park, S.Y.2    Lee, J.K.3    Oh, T.K.4
  • 16
    • 0038481125 scopus 로고    scopus 로고
    • Purification and characterization of cold active lipase from psychrotrophic Aeromonas sp: LPB 4
    • Purification and characterization of cold active lipase from psychrotrophic Aeromonas sp: LPB 4. Lee HK, Ahn MJ, Kwak SH, Song WH, Jeong BC, J Microbiol 2003 41 22 27
    • (2003) J Microbiol , vol.41 , pp. 22-27
    • Lee, H.K.1    Ahn, M.J.2    Kwak, S.H.3    Song, W.H.4    Jeong, B.C.5
  • 18
    • 32544450160 scopus 로고    scopus 로고
    • Characteristics of adjacent family 6 acetylxylan esterases from Fibrobacter succinogenes and the interaction with the Xyn10E xylanase in hydrolysis of acetylated xylan
    • DOI 10.1139/w05-074
    • Characteristics of adjacent family 6 acetylxylan esterases from Fibrobacter succinogenes and the interaction with the Xyn10E xylanase in hydrolysis of acetylated xylan. Kam DK, Jun H-S, Ha JK, Inglis GD, Forsberg CW, Can J Microbiol 2005 51 821 832 10.1139/w05-074 16333341 (Pubitemid 43235359)
    • (2005) Canadian Journal of Microbiology , vol.51 , Issue.10 , pp. 821-832
    • Kam, D.K.1    Jun, H.-S.2    Ha, J.K.3    Inglis, G.D.4    Forsberg, C.W.5
  • 20
    • 0030587498 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of the mono- and diacylglycerol lipase gene (mdlB) of Aspergillus oryzae
    • DOI 10.1016/0378-1097(96)00291-1
    • Cloning and nucleotide sequence of the mono- and diacylglycerol lipase gene (mdlB) of Aspergillus oryzae. Tsuchiya A, Nakazawa H, Toida J, Ohnishi K, Sekiguchi J, FEMS Microbiol Lett 1996 143 63 67 10.1111/j.1574-6968.1996. tb08462.x 8807803 (Pubitemid 26292654)
    • (1996) FEMS Microbiology Letters , vol.143 , Issue.1 , pp. 63-67
    • Tsuchiya, A.1    Nakazawa, H.2    Toida, J.3    Ohnishi, K.4    Sekiguchi, J.5
  • 21
  • 22
    • 0030841912 scopus 로고    scopus 로고
    • Aspergillus as a host for heterologous protein production: The problem of proteases
    • DOI 10.1016/S0167-7799(97)01020-2, PII S0167779997010202
    • Aspergillus as a host for heterologous protein production: the problem of proteases. van den Hombergh JPTW, van de Vondervoort PJI, Fraissinet-Tachet L, Visser J, Trends Biotechnol 1997 15 256 263 10.1016/S0167-7799(97)01020-2 9237405 (Pubitemid 27342095)
    • (1997) Trends in Biotechnology , vol.15 , Issue.7 , pp. 256-263
    • Van Den Hombergh, J.P.T.W.1    Van De Vondervoort, P.J.I.2    Fraissinet-Tachet, L.3    Visser, J.4
  • 23
    • 80053340547 scopus 로고    scopus 로고
    • Curation of characterized glycoside hydrolases of fungal origin
    • 10.1093/database/bar020
    • Curation of characterized glycoside hydrolases of fungal origin. Murphy C, Powlowski J, Wu M, Butler G, Tsang A, Database (Oxford) 2011 2011 ar020 10.1093/database/bar020
    • (2011) Database (Oxford) , vol.2011
    • Murphy, C.1    Powlowski, J.2    Wu, M.3    Butler, G.4    Tsang, A.5
  • 24
    • 0032725633 scopus 로고    scopus 로고
    • The endoplasmic reticulum-gateway of the secretory pathway
    • 10213782
    • The endoplasmic reticulum-gateway of the secretory pathway. Vitale A, Denecke J, Plant Cell 1999 11 615 628 10213782
    • (1999) Plant Cell , vol.11 , pp. 615-628
    • Vitale, A.1    Denecke, J.2
  • 25
    • 84930983004 scopus 로고    scopus 로고
    • Transient expression using agroinfiltration and its applications in molecular farming
    • Dordrecht, Heidelberg, London, New York: Springer Netherlands Wang A, Ma S
    • Transient expression using agroinfiltration and its applications in molecular farming. Menassa R, Ahmad A, Joensuu JJ, Molecular farming in plants: recent advances and future prospects Dordrecht, Heidelberg, London, New York: Springer Netherlands, Wang A, Ma S, 2012 183 198
    • (2012) Molecular Farming in Plants: Recent Advances and Future Prospects , pp. 183-198
    • Menassa, R.1    Ahmad, A.2    Joensuu, J.J.3
  • 26
    • 0028314161 scopus 로고
    • Properties of cold-adapted microorganisms and their potential role in biotechnology
    • DOI 10.1016/0168-1656(94)90093-0
    • Properties of cold-adapted microorganisms and their potential role in biotechnology. Margesin R, Schinner F, J Biotechnol 1994 33 1 14 10.1016/0168-1656(94)90093-0 (Pubitemid 24090899)
    • (1994) Journal of Biotechnology , vol.33 , Issue.1 , pp. 1-14
    • Margesin, R.1
  • 28
    • 84855348694 scopus 로고    scopus 로고
    • Fractionation of triticale, wheat, barley, oats, canola, and mustard straws for the production of carbohydrates and lignins
    • 22197077
    • Fractionation of triticale, wheat, barley, oats, canola, and mustard straws for the production of carbohydrates and lignins. Pronyk C, Mazza G, Bioresour Technol 2012 106 117 124 22197077
    • (2012) Bioresour Technol , vol.106 , pp. 117-124
    • Pronyk, C.1    Mazza, G.2
  • 29
    • 0002044589 scopus 로고
    • The role of ester groups in resistance of plant cell wall polysaccharides to enzymatic hydrolysis
    • 23918082
    • The role of ester groups in resistance of plant cell wall polysaccharides to enzymatic hydrolysis. Grohmann K, Mitchell DJ, Himmel ME, Dale BE, Schroeder HA, Appl Biochem Biotechnol 1989 20-21 45 61 23918082
    • (1989) Appl Biochem Biotechnol , vol.2021 , pp. 45-61
    • Grohmann, K.1    Mitchell, D.J.2    Himmel, M.E.3    Dale, B.E.4    Schroeder, H.A.5
  • 30
    • 83655183347 scopus 로고    scopus 로고
    • The role of acetyl xylan esterase in the solubilization of xylan and enzymatic hydrolysis of wheat straw and giant reed
    • 10.1186/1754-6834-4-1 21269444
    • The role of acetyl xylan esterase in the solubilization of xylan and enzymatic hydrolysis of wheat straw and giant reed. Zhang J, Siika-Aho M, Tenkanen M, Viikari L, Biotechnol Biofuels 2011 4 1 10 10.1186/1754-6834-4-1 21269444
    • (2011) Biotechnol Biofuels , vol.4 , pp. 1-10
    • Zhang, J.1    Siika-Aho, M.2    Tenkanen, M.3    Viikari, L.4
  • 31
    • 77957269758 scopus 로고    scopus 로고
    • Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides
    • 10.1016/j.bbrc.2010.08.136 20816933
    • Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides. Huang YC, Chen GH, Chen YF, Chen WL, Yang CH, Biochem Biophys Res Commun 2010 400 718 723 10.1016/j.bbrc.2010.08.136 20816933
    • (2010) Biochem Biophys Res Commun , vol.400 , pp. 718-723
    • Huang, Y.C.1    Chen, G.H.2    Chen, Y.F.3    Chen, W.L.4    Yang, C.H.5
  • 32
    • 41849103104 scopus 로고    scopus 로고
    • Synergistic enhancement of cellobiohydrolase performance on pretreated corn stover by addition of xylanase and esterase activities
    • DOI 10.1016/j.biortech.2007.09.064, PII S0960852407008115
    • Synergistic enhancement of cellobiohydrolase performance on pretreated corn stover by addition of xylanase and esterase activities. Selig MJ, Knoshaug EP, Adney WS, Himmel ME, Decker SR, Bioresour Technol 2008 99 4997 5005 10.1016/j.biortech.2007.09.064 18006303 (Pubitemid 351503850)
    • (2008) Bioresource Technology , vol.99 , Issue.11 , pp. 4997-5005
    • Selig, M.J.1    Knoshaug, E.P.2    Adney, W.S.3    Himmel, M.E.4    Decker, S.R.5
  • 33
    • 0142130541 scopus 로고    scopus 로고
    • Industrial proteins produced from transgenic plants
    • Dordrecht: Springer Netherlands Hood E, Howard J
    • Industrial proteins produced from transgenic plants. Hood E, Woodard S, Plants as factories for protein production Dordrecht: Springer Netherlands, Hood E, Howard J, 2002 119 135
    • (2002) Plants As Factories for Protein Production , pp. 119-135
    • Hood, E.1    Woodard, S.2
  • 34
    • 32044436929 scopus 로고    scopus 로고
    • Analysis of and function predictions for previously conserved hypothetical or putative proteins in Blochmannia floridanus
    • DOI 10.1186/1471-2180-6-1
    • Generation, annotation, and analysis of an extensive Aspergillus niger EST collection. Semova N, Storms R, John T, Gaudet P, Ulycznyj P, Min XJ, Sun J, Butler G, Tsang A, BMC Microbiol 2006 6 1 10 10.1186/1471-2180-6-1 16401340 (Pubitemid 43197355)
    • (2006) BMC Microbiology , vol.6 , pp. 1
    • Gaudermann, P.1    Vogl, I.2    Zientz, E.3    Silva, F.J.4    Moya, A.5    Gross, R.6    Dandekar, T.7
  • 35
    • 0034979060 scopus 로고    scopus 로고
    • A modified Rp13 gene from rice confers tolerance of the Fusarium graminearum mycotoxin deoxynivalenol to transgenic tobacco
    • DOI 10.1006/pmpp.2001.0326
    • A modified Rpl3 gene from rice confers tolerance of the Fusarium graminearum mycotoxin deoxynivalenol to transgenic tobacco. Harris LJ, Gleddie SC, Physiol Mol Plant Pathol 2001 58 173 181 10.1006/pmpp.2001.0326 (Pubitemid 32568867)
    • (2001) Physiological and Molecular Plant Pathology , vol.58 , Issue.4 , pp. 173-181
    • Harris, L.J.1    Gleddie, S.C.2
  • 36
    • 0023236892 scopus 로고
    • Duplication of CaMV 35S promoter sequences creates a strong enhancer for plant genes
    • Duplication of CaMV 35S promoter sequences creates a strong enhancer for plant genes. Kay R, Chan A, Daly M, McPherson J, Science 1987 236 1299 1302 10.1126/science.236.4806.1299 17770331 (Pubitemid 17087894)
    • (1987) Science , vol.236 , Issue.4806 , pp. 1299-1302
    • Kay, R.1    Chan, A.2    Daly, M.3    McPherson, J.4
  • 37
    • 0021111520 scopus 로고
    • Structure and transcription of the nopaline synthase gene region of T-DNA
    • 10.1093/nar/11.2.369 6298724
    • Structure and transcription of the nopaline synthase gene region of T-DNA. Bevan M, Barnes WM, Chilton MD, Nucleic Acids Res 1983 11 369 385 10.1093/nar/11.2.369 6298724
    • (1983) Nucleic Acids Res , vol.11 , pp. 369-385
    • Bevan, M.1    Barnes, W.M.2    Chilton, M.D.3
  • 38
    • 0034891676 scopus 로고    scopus 로고
    • Enhancers and core promoter elements are essential for the activity of a cryptic gene activation sequence from tobacco, tCUP
    • DOI 10.1007/s004380100478
    • Enhancers and core promoter elements are essential for the activity of a cryptic gene activation sequence from tobacco, tCUP. Wu K, Malik K, Tian L, Hu M, Martin T, Foster E, Brown D, Miki B, Mol Genet Genomics 2001 265 763 770 10.1007/s004380100478 11523793 (Pubitemid 32763290)
    • (2001) Molecular Genetics and Genomics , vol.265 , Issue.5 , pp. 763-770
    • Wu, K.1    Malik, K.2    Tian, L.3    Hu, M.4    Martin, T.5    Foster, E.6    Brown, D.7    Miki, B.8
  • 39
    • 0024297206 scopus 로고
    • Isolation and nucleotide sequence of cDNA clones for the pathogenesis-related proteins PR1a, PR1b and PR1c of Nicotiana tabacum cv: Xanthi nc induced by TMV infection
    • 10.1093/nar/16.20.9861 3186451
    • Isolation and nucleotide sequence of cDNA clones for the pathogenesis-related proteins PR1a, PR1b and PR1c of Nicotiana tabacum cv: Xanthi nc induced by TMV infection. Cutt JR, Dixon DC, Carr JP, Klessig DF, Nucleic Acids Res 1988 16 9861 10.1093/nar/16.20.9861 3186451
    • (1988) Nucleic Acids Res , vol.16 , pp. 9861
    • Cutt, J.R.1    Dixon, D.C.2    Carr, J.P.3    Klessig, D.F.4
  • 40
    • 65549096684 scopus 로고    scopus 로고
    • Optimization of elastin-like polypeptide fusions for expression and purification of recombinant proteins in plants
    • 10.1002/bit.22278 19266472
    • Optimization of elastin-like polypeptide fusions for expression and purification of recombinant proteins in plants. Conley AJ, Joensuu JJ, Jevnikar AM, Menassa R, Brandle JE, Biotechnol Bioeng 2009 103 562 573 10.1002/bit.22278 19266472
    • (2009) Biotechnol Bioeng , vol.103 , pp. 562-573
    • Conley, A.J.1    Joensuu, J.J.2    Jevnikar, A.M.3    Menassa, R.4    Brandle, J.E.5
  • 41
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3 942051
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Bradford MM, Anal Biochem 1976 72 248 254 10.1016/0003-2697(76)90527-3 942051
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 42
    • 79953755883 scopus 로고    scopus 로고
    • Isolation and characterization of a ferulic acid esterase (Fae1A) from the rumen fungus Anaeromyces mucronatus
    • 10.1111/j.1365-2672.2011.04990.x 21362116
    • Isolation and characterization of a ferulic acid esterase (Fae1A) from the rumen fungus Anaeromyces mucronatus. Qi M, Wang P, Selinger LB, Yanke LJ, Forster RJ, McAllister TA, J Appl Microbiol 2011 110 1341 1350 10.1111/j.1365-2672.2011.04990.x 21362116
    • (2011) J Appl Microbiol , vol.110 , pp. 1341-1350
    • Qi, M.1    Wang, P.2    Selinger, L.B.3    Yanke, L.J.4    Forster, R.J.5    McAllister, T.A.6
  • 43
    • 33747150773 scopus 로고    scopus 로고
    • Diversity of plant cell wall esterases in thermophilic and thermotolerant fungi
    • DOI 10.1016/j.jbiotec.2006.04.005, PII S0168165606003142
    • Diversity of plant cell wall esterases in thermophilic and thermotolerant fungi. Ghatora SK, Chadha BS, Saini HS, Bhat MK, Faulds CB, J Biotechnol 2006 125 434 445 10.1016/j.jbiotec.2006.04.005 16713648 (Pubitemid 44223838)
    • (2006) Journal of Biotechnology , vol.125 , Issue.3 , pp. 434-445
    • Ghatora, S.K.1    Chadha, B.S.2    Saini, H.S.3    Bhat, M.K.4    Faulds, C.B.5


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