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Volumn 94, Issue 2, 2012, Pages 399-411

Expression, characterization and structural modelling of a feruloyl esterase from the thermophilic fungus Myceliophthora thermophila

Author keywords

Ferulic acid esterase; Heterologous expression; Myceliophthora thermophila; Pichia pastoris; Structural modelling

Indexed keywords

FERULIC ACID ESTERASE; HETEROLOGOUS EXPRESSION; MYCELIOPHTHORA THERMOPHILA; PICHIA PASTORIS; STRUCTURAL MODELLING;

EID: 84862651303     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3612-9     Document Type: Article
Times cited : (59)

References (55)
  • 2
    • 0002233015 scopus 로고
    • Occurrence of thermophilous microfungi in certain alluvial soils near Nottingham
    • Apinis AE (1963) Occurrence of thermophilous microfungi in certain alluvial soils near Nottingham. Nova Hedwigia 5:57-78
    • (1963) Nova Hedwigia , vol.5 , pp. 57-78
    • Apinis, A.E.1
  • 3
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Bendtsen JD, Nielsen H, von Heijne G, Brunak S (2004) Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340:783-795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 4
    • 38649093655 scopus 로고    scopus 로고
    • Biotechnological applications and potential of fungal feruloyl esterases based on prevalence, classification and biochemical diversity
    • Benoit I, Danchin EGJ, Bleichrodt R-J, de Vries R (2008) Biotechnological applications and potential of fungal feruloyl esterases based on prevalence, classification and biochemical diversity. Biotechnol Lett 30:387-396
    • (2008) Biotechnol Lett , vol.30 , pp. 387-396
    • Benoit, I.1    Danchin, E.G.J.2    Bleichrodt, R.-J.3    De Vries, R.4
  • 5
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • DOI 10.1002/pmic.200300771
    • Blom N, Sicheritz-Ponten T, Gupta R, Gammeltoft S, Brunak S (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4:1633-1649 (Pubitemid 38738322)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, So.5
  • 6
    • 0023767035 scopus 로고
    • The molecular evolution of genes and proteins: A tale of two serines
    • Brenner S (1988) The molecular evolution of genes and proteins: a tale of two serines. Nature 334:528-530
    • (1988) Nature , vol.334 , pp. 528-530
    • Brenner, S.1
  • 9
    • 0038805618 scopus 로고    scopus 로고
    • Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: Identification of the nucleophilic serine
    • Crepin VF, Faulds CB, Connerton IF (2003a) Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: identification of the nucleophilic serine. Protein Expr Purif 29:176-184 (Pubitemid 36720247)
    • (2003) Protein Expression and Purification , vol.29 , Issue.2 , pp. 176-184
    • Crepin, V.F.1    Faulds, C.B.2    Connerton, I.F.3
  • 10
    • 0242417646 scopus 로고    scopus 로고
    • A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition
    • DOI 10.1042/BJ20020917
    • Crepin VF, Faulds CB, Connerton IF (2003b) A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentrationdependent substrate inhibition. Biochem J 370:417-427 (Pubitemid 36315130)
    • (2003) Biochemical Journal , vol.370 , Issue.2 , pp. 417-427
    • Crepin, V.F.1    Faulds, C.B.2    Connerton, I.F.3
  • 11
  • 12
    • 1242292964 scopus 로고    scopus 로고
    • Identification of a type-D feruloyl esterase from Neurospora crassa
    • DOI 10.1007/s00253-003-1466-5
    • Crepin VF, Faulds CB, Connerton IF (2004b) Identification of a type-D feruloyl esterase from Neurospora crassa. Appl Microbiol Biotechnol 63:567-570 (Pubitemid 38230515)
    • (2004) Applied Microbiology and Biotechnology , vol.63 , Issue.5 , pp. 567-570
    • Crepin, V.F.1    Connerton, I.F.2    Faulds, C.B.3
  • 14
    • 34547874249 scopus 로고    scopus 로고
    • Molecular cloning, and characterization of a modular acetyl xylan esterase from the edible straw mushroom Volvariella volvacea
    • DOI 10.1111/j.1574-6968.2007.00844.x
    • Ding S, Cao J, Zhou R, Zheng F (2007) Molecular cloning, and characterization of a modular acetyl xylan esterase from the edible straw mushroom Volvariella volvacea. FEMS Microbiol Lett 274:304-310 (Pubitemid 47256268)
    • (2007) FEMS Microbiology Letters , vol.274 , Issue.2 , pp. 304-310
    • Ding, S.1    Cao, J.2    Zhou, R.3    Zheng, F.4
  • 15
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • DOI 10.1016/S0968-0004(98)01254-7, PII S0968000498012547
    • Dodson G, Wlodawer A (1998) Catalytic triads and their relatives. Trends Biochem Sci 23:347-352 (Pubitemid 28461867)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.9 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 16
    • 24644517613 scopus 로고    scopus 로고
    • Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger
    • DOI 10.1111/j.1742-4658.2005.04849.x
    • Faulds CB, Molina R, Gonzalez R, Husband F, Juge N, Sanz-Aparicio J, Hermoso JA (2005) Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger. FEBS J 272:4362-4371 (Pubitemid 41284410)
    • (2005) FEBS Journal , vol.272 , Issue.17 , pp. 4362-4371
    • Faulds, C.B.1    Molina, R.2    Gonzalez, R.3    Husband, F.4    Juge, N.5    Sanz-Aparicio, J.6    Hermoso, J.A.7
  • 18
    • 0033214507 scopus 로고    scopus 로고
    • A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex
    • DOI 10.1042/0264-6021:3430215
    • Fillingham IJ, Kroon PA, Williamson G, Gilbert HJ, Hazlewood GP (1999) A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulose-hemicellulase complex. Biochem J 343:215-224 (Pubitemid 29473898)
    • (1999) Biochemical Journal , vol.343 , Issue.1 , pp. 215-224
    • Fillingham, I.J.1    Kroon, P.A.2    Williamson, G.3    Gilbert, H.J.4    Hazlewood, G.P.5
  • 19
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis
    • DOI 10.1016/S0092-8674(00)81416-6
    • Fülöp V, Böcskei Z, Polgár L (1998) Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell 94:161-170 (Pubitemid 28348004)
    • (1998) Cell , vol.94 , Issue.2 , pp. 161-170
    • Fulop, V.1    Bocskei, Z.2    Polgar, L.3
  • 20
    • 1542314901 scopus 로고    scopus 로고
    • The feruloyl esterase system of Talaromyces stipitatus: Production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity
    • DOI 10.1016/j.jbiotec.2003.12.003, PII S0168165603003432
    • Garcia-Conesa MT, Crepin VF, Goldson AJ, Williamson G, Cummings NJ, Connerton IF, Faulds CB, Kroon PA (2004) The feruloyl esterase system of Talaromyces stipitatus: production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity. J Biotechnol 108:227-241 (Pubitemid 38299463)
    • (2004) Journal of Biotechnology , vol.108 , Issue.3 , pp. 227-241
    • Garcia-Conesa, M.-T.1    Crepin, V.F.2    Goldson, A.J.3    Williamson, G.4    Cummings, N.J.5    Connerton, I.F.6    Faulds, C.B.7    Kroon, P.A.8
  • 22
    • 77951210908 scopus 로고    scopus 로고
    • Structural and functional characterization of a promiscuous feruloyl esterase (Est1E) from the rumen bacterium Butyrivibrio proteoclasticus
    • Goldstone DC, Villas-Bôas SG, Till M, Kelly WJ, Attwood GT, Arcus VL (2010) Structural and functional characterization of a promiscuous feruloyl esterase (Est1E) from the rumen bacterium Butyrivibrio proteoclasticus. Proteins 78:1457-1469
    • (2010) Proteins , vol.78 , pp. 1457-1469
    • Goldstone, D.C.1    Villas-Bôas, S.G.2    Till, M.3    Kelly, W.J.4    Attwood, G.T.5    Arcus, V.L.6
  • 23
    • 77956032934 scopus 로고    scopus 로고
    • Extracellular carbohydrate esterase from the basidiomycete coprinopsis cinerea released ferulic and acetic acids from xylan
    • Hashimoto K, Kaneko S, Yoshida M (2010) Extracellular carbohydrate esterase from the basidiomycete Coprinopsis cinerea released ferulic and acetic acids from xylan. Biosci Biotechnol Biochem 74:1722-1724
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 1722-1724
    • Hashimoto, K.1    Kaneko, S.2    Yoshida, M.3
  • 24
    • 1842686201 scopus 로고    scopus 로고
    • The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family
    • DOI 10.1016/j.jmb.2004.03.003, PII S002228360400275X
    • Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB (2004) The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family. J Mol Biol 338:495-506 (Pubitemid 38479645)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.3 , pp. 495-506
    • Hermoso, J.A.1    Sanz-Aparicio, J.2    Molina, R.3    Juge, N.4    Gonzalez, R.5    Faulds, C.B.6
  • 26
    • 0035735155 scopus 로고    scopus 로고
    • High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris
    • DOI 10.1016/S1567-1356(01)00020-4, PII S1567135601000204
    • Juge N, Williamson G, Puigserver A, Cummings NJ, Connerton IF, Faulds CB (2001) High level production of recombinant Aspergillus niger cinnamoyl esterase (FAE A) in the methylotrophic yeast Pichia pastoris. FEMS Yeast Res 1:127-132 (Pubitemid 34442281)
    • (2001) FEMS Yeast Research , vol.1 , Issue.2 , pp. 127-132
    • Juge, N.1    Williamson, G.2    Puigserver, A.3    Cummings, N.J.4    Connerton, I.F.5    Faulds, C.B.6
  • 27
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • DOI 10.1093/glycob/cwh151
    • Julenius K, Mølgaard A, Gupta R, Brunak S (2005) Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 15:153-164 (Pubitemid 40227920)
    • (2005) Glycobiology , vol.15 , Issue.2 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 28
    • 37849045248 scopus 로고    scopus 로고
    • The crystal structure of the estA protein, a virulence factor from streptococcus pneumoniae
    • Kim MH, Kang BS, Kim S, Kim KJ, Lee CH, Oh BC, Park SC, Oh TK (2008) The crystal structure of the estA protein, a virulence factor from Streptococcus pneumoniae. Proteins 70:578-583
    • (2008) Proteins , vol.70 , pp. 578-583
    • Kim, M.H.1    Kang, B.S.2    Kim, S.3    Kim, K.J.4    Lee, C.H.5    Oh, B.C.6    Park, S.C.7    Oh, T.K.8
  • 31
    • 67349198849 scopus 로고    scopus 로고
    • Characterization of two distinct feruloyl esterases, AoFaeB and AoFaeC, from Aspergillus oryzae
    • Koseki T, Hori A, Seki S, Murayama T, Shiono Y (2009b) Characterization of two distinct feruloyl esterases, AoFaeB and AoFaeC, from Aspergillus oryzae. Appl Microbiol Biotechnol 83:689-696
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 689-696
    • Koseki, T.1    Hori, A.2    Seki, S.3    Murayama, T.4    Shiono, Y.5
  • 32
    • 0033679102 scopus 로고    scopus 로고
    • A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module
    • Kroon PA, Williamson G, Fish NM, Archer DB, Belshaw NJ (2000) A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module. Eur J Biochem 267:6740-6752
    • (2000) Eur J Biochem , vol.267 , pp. 6740-6752
    • Kroon, P.A.1    Williamson, G.2    Fish, N.M.3    Archer, D.B.4    Belshaw, N.J.5
  • 33
    • 84862705333 scopus 로고    scopus 로고
    • GraFit version 4.0. Erithacus Software Ltd., Staines, UK
    • Leatherbarrow RJ (1998) GraFit version 4.0. Erithacus Software Ltd., Staines, UK
    • (1998)
    • Leatherbarrow, R.J.1
  • 34
    • 0036380565 scopus 로고    scopus 로고
    • Efficient synthesis of 4-methylumbelliferyl dihydroferulate
    • Leschot A, Tapia RA, Eyzaguirre J (2002) Efficient synthesis of 4-methylumbelliferyl dihydroferulate. Synth Commun 32:3219-3223
    • (2002) Synth Commun , vol.32 , pp. 3219-3223
    • Leschot, A.1    Tapia, R.A.2    Eyzaguirre, J.3
  • 35
    • 0037450492 scopus 로고    scopus 로고
    • Two efficient ways to 2-O- and 5-O-feruloylated 4-nitrophenyl α-L-arabinofuranosides as substrates for differentiation of feruloyl esterases
    • DOI 10.1016/S0040-4039(03)00038-8, PII S0040403903000388
    • Mastihubova M, Szemesova J, Biely O (2002) Two efficient ways to 2-O and 5-O-feruloylated 4-nitrophenyl alpha-L-arabinofuranosides as substrates for differentiation of feruloyl esterases. Tetrahedron Lett 44:1671-1673 (Pubitemid 36170110)
    • (2003) Tetrahedron Letters , vol.44 , Issue.8 , pp. 1671-1673
    • Mastihubova, M.1    Szemesova, J.2    Biely, P.3
  • 36
    • 42549139751 scopus 로고    scopus 로고
    • Cloning, characterization and functional expression of an alkalitolerant type C feruloyl esterase from Fusarium oxysporum
    • Moukouli M, Topakas E, Christakopoulos P (2008) Cloning, characterization and functional expression of an alkalitolerant type C feruloyl esterase from Fusarium oxysporum. Appl Microbiol Biotechnol 79:245-254
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 245-254
    • Moukouli, M.1    Topakas, E.2    Christakopoulos, P.3
  • 37
    • 4043115588 scopus 로고    scopus 로고
    • Ferulic acid: Pharmaceutical functions, preparation and applications in foods
    • DOI 10.1002/jsfa.1873
    • Ou S, KwokKC (2004) Ferulic acid: pharmaceutical functions, preparation and applications in foods. J Sci Food Agric 84:1261-1269 (Pubitemid 39059329)
    • (2004) Journal of the Science of Food and Agriculture , vol.84 , Issue.11 , pp. 1261-1269
    • Ou, S.1    Kwok, K.-C.2
  • 38
    • 0028518891 scopus 로고
    • Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger
    • DOI 10.1016/0008-6215(94)00177-4
    • Ralet M-C, Faulds CB, Williamson G, Thibault J-F (1994) Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger. Carbohydr Res 263:257-269 (Pubitemid 24320401)
    • (1994) Carbohydrate Research , vol.263 , Issue.2 , pp. 257-269
    • Ralet, M.-C.1    Faulds, C.B.2    Williamson, G.3    Thibault, J.-F.4
  • 41
    • 33846152664 scopus 로고    scopus 로고
    • A type B feruloyl esterase from Aspergillus nidulans with broad pH applicability
    • DOI 10.1007/s00253-006-0612-2
    • Shin H-D, Chen RR (2007) A type B feruloyl esterase from Aspergillus nidulans with broad pH applicability. Appl Microbiol Biotechnol 73:1323-1330 (Pubitemid 46089505)
    • (2007) Applied Microbiology and Biotechnology , vol.73 , Issue.6 , pp. 1323-1330
    • Shin, H.-D.1    Chen, R.R.2
  • 42
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • DOI 10.1093/nar/gki408
    • Söding J, Biegert A, Lupas AN (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33:W244-W248 (Pubitemid 44529917)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 43
    • 0025211779 scopus 로고
    • Quantification of protein
    • Stoscheck CM (1990) Quantification of protein. Methods Enzymol 182:50-68
    • (1990) Methods Enzymol , vol.182 , pp. 50-68
    • Stoscheck, C.M.1
  • 44
    • 0037626454 scopus 로고    scopus 로고
    • Production and partial characterisation of feruloyl esterase by Sporotrichum thermophile in solid-state fermentation
    • DOI 10.1016/S0032-9592(03)00044-X
    • Topakas E, Kalogeris E, Kekos D, Macris BJ, Christakopoulos P (2003a) Production and partial characterization of feruloyl esterase by Sporotrichum thermophile in solid-state fermentation. Proc Biochem 38:1539-1543 (Pubitemid 36821285)
    • (2003) Process Biochemistry , vol.38 , Issue.11 , pp. 1539-1543
    • Topakas, E.1    Kalogeris, E.2    Kekos, D.3    Macris, B.J.4    Christakopoulos, P.5
  • 45
    • 12244255095 scopus 로고    scopus 로고
    • Purification and characterization of a feruloyl esterase from Fusarium oxysporum catalyzing esterification of phenolic acids in ternary water-organic solvent mixtures
    • DOI 10.1016/S0168-1656(02)00363-2
    • Topakas E, Stamatis H, Biely P, Kekos D, Macris BJ, Christakopoulos P (2003b) Purification and characterization of a feruloyl esterase from Fusarium oxysporum catalyzing esterification of phenolic acids in ternary water-organic solvent mixtures. J Biotechnol 102:33-44 (Pubitemid 36369201)
    • (2003) Journal of Biotechnology , vol.102 , Issue.1 , pp. 33-44
    • Topakas, E.1    Stamatis, H.2    Biely, P.3    Kekos, D.4    Macris, B.J.5    Christakopoulos, P.6
  • 46
    • 0042882381 scopus 로고    scopus 로고
    • Purification and characterization of a Fusarium oxysporum feruloyl esterase (FoFAE-I) catalysing transesterification of phenolic acid esters
    • DOI 10.1016/S0141-0229(03)00213-8
    • Topakas E, Stamatis H, Mastihubova M, Biely P, Kekos D, Macris BJ, Christakopoulos P (2003c) Purification and characterization of a Fusarium oxysporum feruloyl esterase (FoFae-I) catalysing transesterification of phenolic acid esters. Enzyme Microb Technol 33:729-737 (Pubitemid 37088080)
    • (2003) Enzyme and Microbial Technology , vol.33 , Issue.5 , pp. 729-737
    • Topakas, E.1    Stamatis, H.2    Mastihubova, M.3    Biely, P.4    Kekos, D.5    Macris, B.J.6    Christakopoulos, P.7
  • 47
    • 1542359003 scopus 로고    scopus 로고
    • Purification and characterization of a type B feruloyl esterase (StFAE-A) from the thermophilic fungus Sporotrichum thermophile
    • DOI 10.1007/s00253-003-1481-6
    • Topakas E, Stamatis H, Biely P, Christakopoulos P (2004) Purification and characterization of a type B feruloyl esterase (StFAE-A) from the thermophilic fungus Sporotrichum thermophile. Appl Microbiol Biotechnol 63:686-690 (Pubitemid 38316696)
    • (2004) Applied Microbiology and Biotechnology , vol.63 , Issue.6 , pp. 686-690
    • Topakas, E.1    Stamatis, H.2    Biely, P.3    Christakopoulos, P.4
  • 48
    • 14544304535 scopus 로고    scopus 로고
    • Sporotrichum thermophile type C feruloyl esterase (StFaeC): Purification, characterization, and its use for phenolic acid (sugar) ester synthesis
    • DOI 10.1016/j.enzmictec.2004.12.020, PII S0141022904004041
    • Topakas E, Vafiadi C, Stamatis H, Christakopoulos P (2005) Sporotrichum thermophile type C feruloyl esterase (StFaeC): purification characterization, and its use for phenolic acid (sugar) ester synthesis. Enzyme Microb Technol 36:729-736 (Pubitemid 40298894)
    • (2005) Enzyme and Microbial Technology , vol.36 , Issue.5-6 , pp. 729-736
    • Topakas, E.1    Vafiadi, C.2    Stamatis, H.3    Christakopoulos, P.4
  • 49
    • 33947214919 scopus 로고    scopus 로고
    • Microbial production, characterization and applications of feruloyl esterases
    • DOI 10.1016/j.procbio.2007.01.007, PII S1359511307000335
    • Topakas E, Vafiadi C, Christakopoulos P (2007) Microbial production, characterization and applications of feruloyl esterases. Proc Biochem 42:497-509 (Pubitemid 46415793)
    • (2007) Process Biochemistry , vol.42 , Issue.4 , pp. 497-509
    • Topakas, E.1    Vafiadi, C.2    Christakopoulos, P.3
  • 50
    • 78649906497 scopus 로고    scopus 로고
    • The interplay of descriptor-based computational analysis with pharmacophore modeling builds the basis for a novel classification scheme for feruloyl esterases
    • Udatha DBRKG, Kouskoumvekaki I, Olsson L, Panagiotou G (2011) The interplay of descriptor-based computational analysis with pharmacophore modeling builds the basis for a novel classification scheme for feruloyl esterases. Biotechnol Adv 29:94-110
    • (2011) Biotechnol Adv , vol.29 , pp. 94-110
    • Udatha, D.B.R.K.G.1    Kouskoumvekaki, I.2    Olsson, L.3    Panagiotou, G.4
  • 51
    • 12944324721 scopus 로고    scopus 로고
    • Mapping the hydrolytic and synthetic selectivity of a type C feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates
    • DOI 10.1016/j.tetasy.2004.11.037, PII S0957416604008857, Carbohydrate Science. Part 2
    • Vafiadi C, Topakas E, Wong KKY, Suckling ID, Christakopoulos P (2005) Mapping the hydrolytic and synthetic selectivity of a type C feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates. Tetrahedron-Asymmetry 16:373-379 (Pubitemid 40174817)
    • (2005) Tetrahedron Asymmetry , vol.16 , Issue.2 , pp. 373-379
    • Vafiadi, C.1    Topakas, E.2    Wong, K.K.Y.3    Suckling, I.D.4    Christakopoulos, P.5
  • 52
    • 0007881773 scopus 로고
    • The genus Myceliophthora
    • van Oorschot CAN (1977) The genus Myceliophthora. Persoonia 9:401-408
    • (1977) Persoonia , vol.9 , pp. 401-408
    • Van Oorschot, C.A.N.1
  • 53
    • 34250417397 scopus 로고
    • Revision of thermophilic Sporotrichum-spp.: Chrysosporium thermophilum (Apinis) comb. nov. and Chrysosporium fergusil sp. nov. Conidial state of Corynascus thermophilus comb. nov
    • von Klopotek A (1974) Revision of thermophilic Sporotrichum-spp.: Chrysosporium thermophilum (Apinis) comb. nov. and Chrysosporium fergusil sp. nov. Conidial state of Corynascus thermophilus comb. nov. Arch Microbiol 98:365-369
    • (1974) Arch Microbiol , vol.98 , pp. 365-369
    • Von Klopotek, A.1
  • 54
    • 0037406141 scopus 로고    scopus 로고
    • Can correct protein models be identified?
    • Wallner B, Elofsson A (2003) Can correct protein models be identified? Protein Sci 12:1073-1086
    • (2003) Protein Sci , vol.12 , pp. 1073-1068
    • Wallner, B.1    Elofsson, A.2
  • 55
    • 70349335454 scopus 로고    scopus 로고
    • Crystal structure of human esterase D: A potential genetic marker of retinoblastoma
    • Wu D, Li Y, Song G, Zhang D, Shaw N, Liu ZJ (2009) Crystal structure of human esterase D: a potential genetic marker of retinoblastoma. FASEB J 23:1441-1446
    • (2009) FASEB J , vol.23 , pp. 1441-1446
    • Wu, D.1    Li, Y.2    Song, G.3    Zhang, D.4    Shaw, N.5    Liu, Z.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.