메뉴 건너뛰기




Volumn 11, Issue , 2012, Pages

Recombinant sterol esterase from Ophiostoma piceae: an improved biocatalyst expressed in Pichia pastoris

Author keywords

Aggregation behaviour; Catalytic efficiency; N terminal; Ophiostoma piceae; Pichia pastoris; Sterol esterase

Indexed keywords

CHOLESTEROL ESTERASE;

EID: 84870492810     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-11-73     Document Type: Article
Times cited : (28)

References (69)
  • 1
    • 77954660408 scopus 로고    scopus 로고
    • Plant sterol and stanol substrate specificity of pancreatic cholesterol esterase
    • 10.1016/j.jnutbio.2009.04.008, 19615880
    • Brown AW, Hang J, Dussault PH, Carr TP. Plant sterol and stanol substrate specificity of pancreatic cholesterol esterase. J Nutr Biochem 2010, 21:736-740. 10.1016/j.jnutbio.2009.04.008, 19615880.
    • (2010) J Nutr Biochem , vol.21 , pp. 736-740
    • Brown, A.W.1    Hang, J.2    Dussault, P.H.3    Carr, T.P.4
  • 3
    • 0030929823 scopus 로고    scopus 로고
    • Bile salt activation of human cholesterol esterase does not require protein dimerisation
    • 10.1016/S0014-5793(97)00215-9, 9108320
    • Loomes KM, Senior HEJ. Bile salt activation of human cholesterol esterase does not require protein dimerisation. FEBS Lett 1997, 405:369-372. 10.1016/S0014-5793(97)00215-9, 9108320.
    • (1997) FEBS Lett , vol.405 , pp. 369-372
    • Loomes, K.M.1    Senior, H.E.J.2
  • 4
    • 1842831529 scopus 로고    scopus 로고
    • Purification and characterization of a novel cholesterol esterase from Pseudomonas aeruginosa, with its application to cleaning lipid-stained contact lenses
    • 10.1271/bbb.66.2347, 12506971
    • Sugihara A, Shimada Y, Nomura A, Terai T, Imayasu M, Nagai Y, et al. Purification and characterization of a novel cholesterol esterase from Pseudomonas aeruginosa, with its application to cleaning lipid-stained contact lenses. Biosci Biotechnol Biochem 2002, 66:2347-2355. 10.1271/bbb.66.2347, 12506971.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2347-2355
    • Sugihara, A.1    Shimada, Y.2    Nomura, A.3    Terai, T.4    Imayasu, M.5    Nagai, Y.6
  • 5
    • 33646238249 scopus 로고    scopus 로고
    • Novel cholesterol esterase secreted by Streptomyces persists during aqueous long-term storage
    • 10.1263/jbb.101.19, 16503286
    • Xiang H, Takaya N, Hoshino T. Novel cholesterol esterase secreted by Streptomyces persists during aqueous long-term storage. J Biosci Bioeng 2006, 101:19-25. 10.1263/jbb.101.19, 16503286.
    • (2006) J Biosci Bioeng , vol.101 , pp. 19-25
    • Xiang, H.1    Takaya, N.2    Hoshino, T.3
  • 6
  • 7
    • 0032530679 scopus 로고    scopus 로고
    • Candida rugosa lipases: molecular biology and versatility in biotechnology
    • 10.1002/(SICI)1097-0061(19980915)14:12<1069::AID-YEA303>3.0.CO;2-K, 9778794
    • Benjamin S, Pandey A. Candida rugosa lipases: molecular biology and versatility in biotechnology. Yeast 1998, 14:1069-1087. 10.1002/(SICI)1097-0061(19980915)14:12<1069::AID-YEA303>3.0.CO;2-K, 9778794.
    • (1998) Yeast , vol.14 , pp. 1069-1087
    • Benjamin, S.1    Pandey, A.2
  • 8
    • 33748414191 scopus 로고    scopus 로고
    • Efficient production of active recombinant Candida rugosa LIP3 lipase in Pichia pastoris and biochemical characterization of purified enzyme
    • 10.1021/jf060835e, 16881684
    • Chang SW, Lee GC, Shaw JF. Efficient production of active recombinant Candida rugosa LIP3 lipase in Pichia pastoris and biochemical characterization of purified enzyme. J Agric Food Chem 2006, 54:5831-5838. 10.1021/jf060835e, 16881684.
    • (2006) J Agric Food Chem , vol.54 , pp. 5831-5838
    • Chang, S.W.1    Lee, G.C.2    Shaw, J.F.3
  • 9
    • 0034773014 scopus 로고    scopus 로고
    • Production of native and recombinant lipases by Candida rugosa - a review
    • 10.1385/ABAB:95:3:221, 11732718
    • Ferrer P, Montesinos JL, Valero F, Solá C. Production of native and recombinant lipases by Candida rugosa - a review. Appl Biochem Biotechnol 2001, 95:221-255. 10.1385/ABAB:95:3:221, 11732718.
    • (2001) Appl Biochem Biotechnol , vol.95 , pp. 221-255
    • Ferrer, P.1    Montesinos, J.L.2    Valero, F.3    Solá, C.4
  • 10
    • 67651115521 scopus 로고    scopus 로고
    • Recombinant Candida rugosa LIP2 expression in Pichia pastoris under the control of the AOX1 promoter
    • Ferrer P, Alarcón M, Ramón R, Benaiges MD, Valero F. Recombinant Candida rugosa LIP2 expression in Pichia pastoris under the control of the AOX1 promoter. Biochem Eng J 2009, 46:271-277.
    • (2009) Biochem Eng J , vol.46 , pp. 271-277
    • Ferrer, P.1    Alarcón, M.2    Ramón, R.3    Benaiges, M.D.4    Valero, F.5
  • 11
    • 5044236206 scopus 로고    scopus 로고
    • Reactivity of pure Candida rugosa lipase isoenzymes (Lip1, Lip2, and Lip3) in aqueous and organic media. Influence of the isoenzymatic profile on the lipase performance in organic media
    • López N, Pernas MA, Pastrana LM, Sánchez A, Valero F, Rúa ML. Reactivity of pure Candida rugosa lipase isoenzymes (Lip1, Lip2, and Lip3) in aqueous and organic media. Influence of the isoenzymatic profile on the lipase performance in organic media. Biotechnol Prog 2004, 20:65-73.
    • (2004) Biotechnol Prog , vol.20 , pp. 65-73
    • López, N.1    Pernas, M.A.2    Pastrana, L.M.3    Sánchez, A.4    Valero, F.5    Rúa, M.L.6
  • 12
    • 0042386531 scopus 로고    scopus 로고
    • Structural insiesterase behaviour in the/esterase behaviour in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97 Å resolution.
    • 10.1016/j.jmb.2003.08.005, 14499609
    • Mancheño JM, Pernas MA, Martínez MJ, Ochoa B, Rúa ML, Hermoso JA. Structural insiesterase behaviour in the/esterase behaviour in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97 Å resolution. J Mol Biol 2003, 332:1059-1069. 10.1016/j.jmb.2003.08.005, 14499609.
    • (2003) J Mol Biol , vol.332 , pp. 1059-1069
    • Mancheño, J.M.1    Pernas, M.A.2    Martínez, M.J.3    Ochoa, B.4    Rúa, M.L.5    Hermoso, J.A.6
  • 13
    • 0037209774 scopus 로고    scopus 로고
    • Hydrolysis of steryl esters by a lipase (Lip 3) from Candida rugosa
    • 10.1007/s00253-002-1063-z, 12382052
    • Tenkanen M, Kontkanen H, Isoniemi R, Spetz P, Holmbom B. Hydrolysis of steryl esters by a lipase (Lip 3) from Candida rugosa. Appl Microbiol Biotechnol 2002, 60:120-127. 10.1007/s00253-002-1063-z, 12382052.
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 120-127
    • Tenkanen, M.1    Kontkanen, H.2    Isoniemi, R.3    Spetz, P.4    Holmbom, B.5
  • 14
    • 78049287825 scopus 로고    scopus 로고
    • Site-specific saturation mutagenesis on residues 132 and 450 of Candida rugosa LIP2 enhances catalytic efficiency and alters substrate specificity in various chain lengths of triglycerides and esters
    • Yen CC, Malmis CC, Lee GC, Lee LC, Shaw JF. Site-specific saturation mutagenesis on residues 132 and 450 of Candida rugosa LIP2 enhances catalytic efficiency and alters substrate specificity in various chain lengths of triglycerides and esters. J Agric Food Chem 2010, 58:10899-10905.
    • (2010) J Agric Food Chem , vol.58 , pp. 10899-10905
    • Yen, C.C.1    Malmis, C.C.2    Lee, G.C.3    Lee, L.C.4    Shaw, J.F.5
  • 15
    • 33745196238 scopus 로고    scopus 로고
    • Cloning and expression of a Melanocarpus albomyces steryl esterase gene in Pichia pastoris and Trichoderma reesei
    • 10.1002/bit.20686, 16615142
    • Kontkanen H, Reinikainen T, Saloheimo M. Cloning and expression of a Melanocarpus albomyces steryl esterase gene in Pichia pastoris and Trichoderma reesei. Biotechnol Bioeng 2006, 94:407-415. 10.1002/bit.20686, 16615142.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 407-415
    • Kontkanen, H.1    Reinikainen, T.2    Saloheimo, M.3
  • 16
    • 43549123793 scopus 로고    scopus 로고
    • Characterization of novel cholesterol esterase from Trichoderma sp AS59 with high ability to synthesize steryl esters
    • 10.1263/jbb.105.341, 18499049
    • Maeda A, Mizuno T, Bunya M, Sugihara S, Nakayama D, Tsunasawa S, et al. Characterization of novel cholesterol esterase from Trichoderma sp AS59 with high ability to synthesize steryl esters. J Biosci Bioeng 2008, 105:341-349. 10.1263/jbb.105.341, 18499049.
    • (2008) J Biosci Bioeng , vol.105 , pp. 341-349
    • Maeda, A.1    Mizuno, T.2    Bunya, M.3    Sugihara, S.4    Nakayama, D.5    Tsunasawa, S.6
  • 17
    • 0032784276 scopus 로고    scopus 로고
    • α/β hydrolase fold enzymes: the family keeps growing
    • 10.1016/S0959-440X(99)00037-8, 10607665
    • Nardini M, Dijkstra BW. α/β hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol 1999, 9:732-737. 10.1016/S0959-440X(99)00037-8, 10607665.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 18
    • 78649675664 scopus 로고    scopus 로고
    • Purification and characterization of novel extracellular cholesterol esterase from Acinetobacter sp
    • 10.1002/jobm.200900292, 20473956
    • Du L, Huo Y, Ge F, Yu J, Li W, Cheng G, et al. Purification and characterization of novel extracellular cholesterol esterase from Acinetobacter sp. J Basic Microbiol 2010, 50:S30-S36. 10.1002/jobm.200900292, 20473956.
    • (2010) J Basic Microbiol , vol.50
    • Du, L.1    Huo, Y.2    Ge, F.3    Yu, J.4    Li, W.5    Cheng, G.6
  • 20
    • 0035854699 scopus 로고    scopus 로고
    • Influence of the conformational flexibility on the kinetics and dimerisation process of two Candida rugosa lipase isoenzymes
    • 10.1016/S0014-5793(01)02630-8, 11457462
    • Pernas MA, López C, Rúa ML, Hermoso J. Influence of the conformational flexibility on the kinetics and dimerisation process of two Candida rugosa lipase isoenzymes. FEBS Lett 2001, 501:87-91. 10.1016/S0014-5793(01)02630-8, 11457462.
    • (2001) FEBS Lett , vol.501 , pp. 87-91
    • Pernas, M.A.1    López, C.2    Rúa, M.L.3    Hermoso, J.4
  • 21
    • 33646501967 scopus 로고    scopus 로고
    • Purification and characterisation of a novel steryl esterase from Melanocarpus albomyces
    • Kontkanen H, Tenkanen M, Reinikainen T. Purification and characterisation of a novel steryl esterase from Melanocarpus albomyces. Enzyme Microb Technol 2006, 39:265-273.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 265-273
    • Kontkanen, H.1    Tenkanen, M.2    Reinikainen, T.3
  • 24
    • 0013249985 scopus 로고    scopus 로고
    • Lipase production by Penicillium restrictum using solid waste of industrial babassu oil production as substrate
    • Palma MB, Pinto AL, Gombert AK, Seitz KH, Kivatinitz SC, Castilho LR, et al. Lipase production by Penicillium restrictum using solid waste of industrial babassu oil production as substrate. Appl Biochem Biotechnol 2000, 84-86:1137-1145.
    • (2000) Appl Biochem Biotechnol , vol.84-86 , pp. 1137-1145
    • Palma, M.B.1    Pinto, A.L.2    Gombert, A.K.3    Seitz, K.H.4    Kivatinitz, S.C.5    Castilho, L.R.6
  • 25
    • 0032852741 scopus 로고    scopus 로고
    • Recombinant microbial lipases for biotechnological applications
    • 10.1016/S0968-0896(99)00141-8, 10579516
    • Schmidt-Dannert C. Recombinant microbial lipases for biotechnological applications. Bioorg Med Chem 1999, 7:2123-2130. 10.1016/S0968-0896(99)00141-8, 10579516.
    • (1999) Bioorg Med Chem , vol.7 , pp. 2123-2130
    • Schmidt-Dannert, C.1
  • 26
    • 0028827506 scopus 로고
    • Review: methylotrophic yeast as factories for the production of foreign proteins
    • 10.1002/yea.320111402, 8585317
    • Faber KN, Harder W, Ab G, Veenhuis M. Review: methylotrophic yeast as factories for the production of foreign proteins. Yeast 1995, 11:1331-1344. 10.1002/yea.320111402, 8585317.
    • (1995) Yeast , vol.11 , pp. 1331-1344
    • Faber, K.N.1    Harder, W.2    Ab, G.3    Veenhuis, M.4
  • 28
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • 10.1002/yea.1208, 15704221
    • Macauley-Patrick S, Fazenda ML, McNeil B, Harvey LM. Heterologous protein production using the Pichia pastoris expression system. Yeast 2005, 22:249-270. 10.1002/yea.1208, 15704221.
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 29
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • 10.1111/j.1574-6976.2000.tb00532.x, 10640598
    • Cereghino JL, Cregg JM. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol Rev 2000, 24:45-66. 10.1111/j.1574-6976.2000.tb00532.x, 10640598.
    • (2000) FEMS Microbiol Rev , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 30
    • 67149116767 scopus 로고    scopus 로고
    • Genome sequence of the recombinant protein production host Pichia pastoris
    • 10.1038/nbt.1544, 19465926
    • De Schutter K, Lin YC, Tiels P, Van Hecke A, Glinka S, Weber-Lehmann J, et al. Genome sequence of the recombinant protein production host Pichia pastoris. Nat Biotechnol 2009, 27:561-566. 10.1038/nbt.1544, 19465926.
    • (2009) Nat Biotechnol , vol.27 , pp. 561-566
    • De Schutter, K.1    Lin, Y.C.2    Tiels, P.3    Van Hecke, A.4    Glinka, S.5    Weber-Lehmann, J.6
  • 34
    • 8744296151 scopus 로고    scopus 로고
    • Hydrolysis of sterol esters by an esterase from Ophiostoma piceae: application for pitch control in pulping of Eucalyptus globulus wood
    • Calero-Rueda O, Gutiérrez A, del Río JC, Prieto A, Plou FJ, Ballesteros A, et al. Hydrolysis of sterol esters by an esterase from Ophiostoma piceae: application for pitch control in pulping of Eucalyptus globulus wood. Int J Biotechnol 2004, 6:367-375.
    • (2004) Int J Biotechnol , vol.6 , pp. 367-375
    • Calero-Rueda, O.1    Gutiérrez, A.2    del Río, J.C.3    Prieto, A.4    Plou, F.J.5    Ballesteros, A.6
  • 37
    • 0036168995 scopus 로고    scopus 로고
    • Dichroweb: an interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • 10.1093/bioinformatics/18.1.211, 11836237
    • Lobley A, Whitmore L, Wallace BA. Dichroweb: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002, 18:211-212. 10.1093/bioinformatics/18.1.211, 11836237.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 38
    • 4444290944 scopus 로고    scopus 로고
    • Recombinant expression of Ole e 6, a Cys-enriched pollen allergen, in Pichia pastoris yeast: detection of partial oxidation of methionine by NMR
    • 10.1016/j.pep.2004.06.012, 15358355
    • Barral P, Tejera ML, Treviño MA, Batanero E, Villalba M, Bruix M, et al. Recombinant expression of Ole e 6, a Cys-enriched pollen allergen, in Pichia pastoris yeast: detection of partial oxidation of methionine by NMR. Protein Expr Purif 2004, 37:336-343. 10.1016/j.pep.2004.06.012, 15358355.
    • (2004) Protein Expr Purif , vol.37 , pp. 336-343
    • Barral, P.1    Tejera, M.L.2    Treviño, M.A.3    Batanero, E.4    Villalba, M.5    Bruix, M.6
  • 39
    • 0038128640 scopus 로고    scopus 로고
    • Expression of Sonic hedgehog-Fc fusion protein in Pichia pastoris. Identification and control of post-translational, chemical, and proteolytic modifications
    • 10.1016/S1046-5928(03)00062-7, 12767820
    • Shapiro RI, Wen D, Levesque M, Hronowski X, Gill A, Garber EA, et al. Expression of Sonic hedgehog-Fc fusion protein in Pichia pastoris. Identification and control of post-translational, chemical, and proteolytic modifications. Protein Expr Purif 2003, 29:272-283. 10.1016/S1046-5928(03)00062-7, 12767820.
    • (2003) Protein Expr Purif , vol.29 , pp. 272-283
    • Shapiro, R.I.1    Wen, D.2    Levesque, M.3    Hronowski, X.4    Gill, A.5    Garber, E.A.6
  • 40
    • 0031777548 scopus 로고    scopus 로고
    • Design, total synthesis, and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase
    • 10.1002/pro.5560070618, 2144025, 9655346
    • Brocca S, Schmidt-Dannert C, Lotti M, Alberghina L, Schmid RD. Design, total synthesis, and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase. Protein Sci 1998, 7:1415-1422. 10.1002/pro.5560070618, 2144025, 9655346.
    • (1998) Protein Sci , vol.7 , pp. 1415-1422
    • Brocca, S.1    Schmidt-Dannert, C.2    Lotti, M.3    Alberghina, L.4    Schmid, R.D.5
  • 41
    • 33244490497 scopus 로고    scopus 로고
    • Codon optimization of Candida rugosa lip1 gene for improving expression in Pichia pastoris and biochemical characterization of the purified recombinant LIP1 lipase
    • 10.1021/jf052183k, 16448188
    • Chang SW, Lee GC, Shaw JF. Codon optimization of Candida rugosa lip1 gene for improving expression in Pichia pastoris and biochemical characterization of the purified recombinant LIP1 lipase. J Agric Food Chem 2006, 54:815-822. 10.1021/jf052183k, 16448188.
    • (2006) J Agric Food Chem , vol.54 , pp. 815-822
    • Chang, S.W.1    Lee, G.C.2    Shaw, J.F.3
  • 42
    • 0036714663 scopus 로고    scopus 로고
    • Multiple mutagenesis of non-universal serine codons of the Candida rugosa lip2 gene and biochemical characterization of purified recombinant LIP2 lipase overexpressed in Pichia pastoris
    • 10.1042/BJ20020404, 1222792, 12020350
    • Lee GC, Lee LC, Sava V, Shaw JF. Multiple mutagenesis of non-universal serine codons of the Candida rugosa lip2 gene and biochemical characterization of purified recombinant LIP2 lipase overexpressed in Pichia pastoris. Biochem J 2002, 366:603-611. 10.1042/BJ20020404, 1222792, 12020350.
    • (2002) Biochem J , vol.366 , pp. 603-611
    • Lee, G.C.1    Lee, L.C.2    Sava, V.3    Shaw, J.F.4
  • 43
    • 0035264178 scopus 로고    scopus 로고
    • Recombinant expression and characterization of the Candida rugosa LIP4 lipase in Pichia pastoris: comparison of glycosylation, activity, and stability
    • 10.1006/abbi.2000.2235, 11368188
    • Tang SJ, Shaw JF, Sun KH, Sun GH, Chang TY, Lin CK, et al. Recombinant expression and characterization of the Candida rugosa LIP4 lipase in Pichia pastoris: comparison of glycosylation, activity, and stability. Arch Biochem Biophys 2001, 387:93-98. 10.1006/abbi.2000.2235, 11368188.
    • (2001) Arch Biochem Biophys , vol.387 , pp. 93-98
    • Tang, S.J.1    Shaw, J.F.2    Sun, K.H.3    Sun, G.H.4    Chang, T.Y.5    Lin, C.K.6
  • 44
    • 80053503843 scopus 로고    scopus 로고
    • Characterization of codon-optimized recombinant Candida rugosa lipase 5 (LIP5)
    • 10.1021/jf202161a, 21854055
    • Lee LC, Yen CC, Malmis CC, Chen LF, Chen JC, Lee GC, et al. Characterization of codon-optimized recombinant Candida rugosa lipase 5 (LIP5). J Agric Food Chem 2011, 59:10693-10698. 10.1021/jf202161a, 21854055.
    • (2011) J Agric Food Chem , vol.59 , pp. 10693-10698
    • Lee, L.C.1    Yen, C.C.2    Malmis, C.C.3    Chen, L.F.4    Chen, J.C.5    Lee, G.C.6
  • 45
    • 0030801251 scopus 로고    scopus 로고
    • Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: high-level production and some properties of functional expressed lipase B
    • Catoni E, Schmidt-Dannert C, Brocca S, Schmid RD. Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: high-level production and some properties of functional expressed lipase B. Biotechnol Tech 1997, 11:689-695.
    • (1997) Biotechnol Tech , vol.11 , pp. 689-695
    • Catoni, E.1    Schmidt-Dannert, C.2    Brocca, S.3    Schmid, R.D.4
  • 46
    • 0031259834 scopus 로고    scopus 로고
    • High-level production of recombinant Geotrichum candidum lipases in yeast Pichia pastoris
    • 10.1006/prep.1997.0747, 9325136
    • Holmquist M, Tessier DC, Cygler M. High-level production of recombinant Geotrichum candidum lipases in yeast Pichia pastoris. Protein Expr Purif 1997, 11:35-40. 10.1006/prep.1997.0747, 9325136.
    • (1997) Protein Expr Purif , vol.11 , pp. 35-40
    • Holmquist, M.1    Tessier, D.C.2    Cygler, M.3
  • 49
    • 0242662478 scopus 로고    scopus 로고
    • Macrokinetic model for methylotrophic Pichia pastoris based on stoichiometric balance
    • 10.1016/j.jbiotec.2003.08.003, 14636710
    • Ren HT, Yuan JQ, Bellgardt K-H. Macrokinetic model for methylotrophic Pichia pastoris based on stoichiometric balance. J Biotechnol 2003, 106:53-68. 10.1016/j.jbiotec.2003.08.003, 14636710.
    • (2003) J Biotechnol , vol.106 , pp. 53-68
    • Ren, H.T.1    Yuan, J.Q.2    Bellgardt, K.-H.3
  • 50
    • 0035703883 scopus 로고    scopus 로고
    • Non-repressing carbon sources for alcohol oxidase (AOX1) promoter of Pichia pastoris
    • Inan M, Meagher MM. Non-repressing carbon sources for alcohol oxidase (AOX1) promoter of Pichia pastoris. J Biosci Bioeng 2001, 92:585-589.
    • (2001) J Biosci Bioeng , vol.92 , pp. 585-589
    • Inan, M.1    Meagher, M.M.2
  • 51
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
    • 10.1002/jmr.687, 15565717
    • Daly R, Hearn MTW. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J Mol Recognit 2005, 18:119-138. 10.1002/jmr.687, 15565717.
    • (2005) J Mol Recognit , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 52
    • 0035735155 scopus 로고    scopus 로고
    • High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris
    • 10.1111/j.1567-1364.2001.tb00023.x, 12702357
    • Juge N, Williamson G, Puigserver A, Cummings NJ, Connerton IF, Faulds CB. High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris. FEMS Yeast Res 2001, 1:127-132. 10.1111/j.1567-1364.2001.tb00023.x, 12702357.
    • (2001) FEMS Yeast Res , vol.1 , pp. 127-132
    • Juge, N.1    Williamson, G.2    Puigserver, A.3    Cummings, N.J.4    Connerton, I.F.5    Faulds, C.B.6
  • 53
    • 52949132991 scopus 로고    scopus 로고
    • Expression of Candida antarctica lipase B in Pichia pastoris and various Escherichia coli systems
    • 10.1016/j.pep.2008.07.012, 18725303
    • Larsen MW, Bornscheuer UT, Hult K. Expression of Candida antarctica lipase B in Pichia pastoris and various Escherichia coli systems. Protein Expr Purif 2008, 62:90-97. 10.1016/j.pep.2008.07.012, 18725303.
    • (2008) Protein Expr Purif , vol.62 , pp. 90-97
    • Larsen, M.W.1    Bornscheuer, U.T.2    Hult, K.3
  • 54
    • 0030997654 scopus 로고    scopus 로고
    • Strategies for optimal synthesis and secretion of heterologous proteins in the methylotrophic yeast Pichia pastoris
    • 10.1016/S0378-1119(96)00672-5, 9185849
    • Sreekrishna K, Brankamp RG, Kropp KE, Blankenship DT, Tsay JT, Smith PL, et al. Strategies for optimal synthesis and secretion of heterologous proteins in the methylotrophic yeast Pichia pastoris. Gene 1997, 190:55-62. 10.1016/S0378-1119(96)00672-5, 9185849.
    • (1997) Gene , vol.190 , pp. 55-62
    • Sreekrishna, K.1    Brankamp, R.G.2    Kropp, K.E.3    Blankenship, D.T.4    Tsay, J.T.5    Smith, P.L.6
  • 55
    • 0024368268 scopus 로고
    • Secretion of heterologous proteins directed by the yeast α-factor leader
    • Biotechnology series
    • Brake AJ. Secretion of heterologous proteins directed by the yeast α-factor leader. Yeast Genetic Engineering 1989, 269-280. Biotechnology series.
    • (1989) Yeast Genetic Engineering , pp. 269-280
    • Brake, A.J.1
  • 56
    • 0038805618 scopus 로고    scopus 로고
    • Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: identification of the nucleophilic serine
    • 10.1016/S1046-5928(03)00050-0, 12767807
    • Crepin VF, Faulds CB, Connerton IF. Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: identification of the nucleophilic serine. Protein Expr Purif 2003, 29:176-184. 10.1016/S1046-5928(03)00050-0, 12767807.
    • (2003) Protein Expr Purif , vol.29 , pp. 176-184
    • Crepin, V.F.1    Faulds, C.B.2    Connerton, I.F.3
  • 57
    • 0142061109 scopus 로고    scopus 로고
    • Optimized expression of a thermostable xylanase from Thermomyces lanuginosus in Pichia pastoris
    • 10.1128/AEM.69.10.6064-6072.2003, 201252, 14532063
    • Damaso MCT, Almeida MS, Kurtenbach E, Martins OB, Pereira N, Andrade CMMC, et al. Optimized expression of a thermostable xylanase from Thermomyces lanuginosus in Pichia pastoris. Appl Environ Microbiol 2003, 69:6064-6072. 10.1128/AEM.69.10.6064-6072.2003, 201252, 14532063.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6064-6072
    • Damaso, M.C.T.1    Almeida, M.S.2    Kurtenbach, E.3    Martins, O.B.4    Pereira, N.5    Andrade, C.M.M.C.6
  • 58
    • 2942549046 scopus 로고    scopus 로고
    • High-level expression of Candida parapsilosis lipase/acyltransferase in Pichia pastoris
    • 10.1016/j.jbiotec.2004.03.007, 15196768
    • Brunel L, Neugnot V, Landucci L, Boze WN, Moulin G, Bigey F, et al. High-level expression of Candida parapsilosis lipase/acyltransferase in Pichia pastoris. J Biotechnol 2004, 111:41-50. 10.1016/j.jbiotec.2004.03.007, 15196768.
    • (2004) J Biotechnol , vol.111 , pp. 41-50
    • Brunel, L.1    Neugnot, V.2    Landucci, L.3    Boze, W.N.4    Moulin, G.5    Bigey, F.6
  • 59
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: a review
    • 10.1002/yea.320080602, 1502852
    • Romanos MA, Scorer CA, Clare JJ. Foreign gene expression in yeast: a review. Yeast 1992, 8:423-488. 10.1002/yea.320080602, 1502852.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3
  • 60
    • 33749023850 scopus 로고    scopus 로고
    • Characterization of Melanocarpus albomyces steryl esterase produced in Trichoderma reesei and modification of fibre products with the enzyme
    • 10.1007/s00253-006-0321-x, 16470365
    • Kontkanen H, Saloheimo M, Pere J, Miettinen-Oinonen A, Reinikainen T. Characterization of Melanocarpus albomyces steryl esterase produced in Trichoderma reesei and modification of fibre products with the enzyme. Appl Microbiol Biotechnol 2006, 72:696-704. 10.1007/s00253-006-0321-x, 16470365.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 696-704
    • Kontkanen, H.1    Saloheimo, M.2    Pere, J.3    Miettinen-Oinonen, A.4    Reinikainen, T.5
  • 61
    • 0037936790 scopus 로고    scopus 로고
    • General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality
    • 10.1021/bm025729+, 12523838
    • Palomo JM, Fuentes M, Fernández-Lorente G, Mateo C, Guisán JM, Fernández-Lafuente R. General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality. Biomacromolecules 2003, 4:1-6. 10.1021/bm025729+, 12523838.
    • (2003) Biomacromolecules , vol.4 , pp. 1-6
    • Palomo, J.M.1    Fuentes, M.2    Fernández-Lorente, G.3    Mateo, C.4    Guisán, J.M.5    Fernández-Lafuente, R.6
  • 62
    • 0032432466 scopus 로고    scopus 로고
    • Aggregation behaviour of Candida rugosa lipase
    • Liou YC, Marangoni AG, Yada RY. Aggregation behaviour of Candida rugosa lipase. Food Res Int 1998, 31:243-248.
    • (1998) Food Res Int , vol.31 , pp. 243-248
    • Liou, Y.C.1    Marangoni, A.G.2    Yada, R.Y.3
  • 63
    • 0030616306 scopus 로고    scopus 로고
    • Thermoalkalophilic lipase of Bacillus thermocatenulatus. Large-scale production, purification and properties: aggregation behaviour and its effect on activity
    • 10.1016/S0168-1656(97)00079-5, 9304872
    • Rúa ML, Schmidt-Dannert C, Wahl S, Sprauer A, Schmid RD. Thermoalkalophilic lipase of Bacillus thermocatenulatus. Large-scale production, purification and properties: aggregation behaviour and its effect on activity. J Biotechnol 1997, 56:89-102. 10.1016/S0168-1656(97)00079-5, 9304872.
    • (1997) J Biotechnol , vol.56 , pp. 89-102
    • Rúa, M.L.1    Schmidt-Dannert, C.2    Wahl, S.3    Sprauer, A.4    Schmid, R.D.5
  • 64
    • 33747391507 scopus 로고    scopus 로고
    • Expression and purification of two lipases from Yarrowia lipolytica AS 2.1216
    • 10.1016/j.pep.2006.02.007, 16624574
    • Song HT, Jiang ZB, Ma LX. Expression and purification of two lipases from Yarrowia lipolytica AS 2.1216. Protein Expr Purif 2006, 47:393-397. 10.1016/j.pep.2006.02.007, 16624574.
    • (2006) Protein Expr Purif , vol.47 , pp. 393-397
    • Song, H.T.1    Jiang, Z.B.2    Ma, L.X.3
  • 65
    • 68649091229 scopus 로고    scopus 로고
    • Rhizopus chinensis lipase: gene cloning, expression in Pichia pastoris and properties
    • Yu XW, Wang LL, Xu Y. Rhizopus chinensis lipase: gene cloning, expression in Pichia pastoris and properties. J Mol Catal B: Enzym 2009, 57:304-311.
    • (2009) J Mol Catal B: Enzym , vol.57 , pp. 304-311
    • Yu, X.W.1    Wang, L.L.2    Xu, Y.3
  • 66
    • 9644275365 scopus 로고    scopus 로고
    • Role of the N-terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family
    • 10.1016/j.jmb.2004.10.035, 15581894
    • Mandrich L, Merone L, Pezzullo M, Cipolla L, Nicotra F, Rossi M, et al. Role of the N-terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family. J Mol Biol 2005, 345:501-512. 10.1016/j.jmb.2004.10.035, 15581894.
    • (2005) J Mol Biol , vol.345 , pp. 501-512
    • Mandrich, L.1    Merone, L.2    Pezzullo, M.3    Cipolla, L.4    Nicotra, F.5    Rossi, M.6
  • 67
    • 29644442942 scopus 로고    scopus 로고
    • Secretion of pro- and mature Rhizopus arrhizus lipases by Pichia pastoris and properties of the proteins
    • 10.1385/MB:32:1:073, 16382184
    • Niu W, Li Z, Tan T. Secretion of pro- and mature Rhizopus arrhizus lipases by Pichia pastoris and properties of the proteins. Mol Biotechnol 2006, 32:73-81. 10.1385/MB:32:1:073, 16382184.
    • (2006) Mol Biotechnol , vol.32 , pp. 73-81
    • Niu, W.1    Li, Z.2    Tan, T.3
  • 68
    • 72149092411 scopus 로고    scopus 로고
    • Differences in biocatalytic behaviour between two variants of StcI esterase from Aspergillus nidulans and its potential use in biocatalysis
    • Peña-Montes C, Lange S, Castro-Ochoa D, Ruiz-Noria K, Cruz-García F, Schmid R, et al. Differences in biocatalytic behaviour between two variants of StcI esterase from Aspergillus nidulans and its potential use in biocatalysis. J Mol Catal B: Enzym 2009, 61:225-234.
    • (2009) J Mol Catal B: Enzym , vol.61 , pp. 225-234
    • Peña-Montes, C.1    Lange, S.2    Castro-Ochoa, D.3    Ruiz-Noria, K.4    Cruz-García, F.5    Schmid, R.6
  • 69
    • 13844278305 scopus 로고    scopus 로고
    • N-terminal peptide of Rhizopus oryzae lipase is important for its catalytic properties
    • 10.1016/j.febslet.2004.12.068, 15710378
    • Sayari A, Frikha F, Miled N, Mtibaa H, Ali YB, Verger R, et al. N-terminal peptide of Rhizopus oryzae lipase is important for its catalytic properties. FEBS Lett 2005, 579:976-982. 10.1016/j.febslet.2004.12.068, 15710378.
    • (2005) FEBS Lett , vol.579 , pp. 976-982
    • Sayari, A.1    Frikha, F.2    Miled, N.3    Mtibaa, H.4    Ali, Y.B.5    Verger, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.