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Volumn 76, Issue 3, 2007, Pages 579-585

De novo synthesis, constitutive expression of Aspergillus sulphureus β-xylanase gene in Pichia pastoris and partial enzymic characterization

Author keywords

Aspergillus sulphureus; Constitutive expression; De novo synthesis; Endo 1, 4 xylanase; Pichia pastoris

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CATALYST ACTIVITY; FERMENTATION; GENE EXPRESSION;

EID: 34548012364     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-0978-9     Document Type: Article
Times cited : (24)

References (22)
  • 1
    • 0034084579 scopus 로고    scopus 로고
    • High-level production of recombinant fungal endo-beta-1,4-xylanases in the methylotrophic yeast Pichia pastoris
    • Berrin JG, Williamson G, Puigserver A, Chaix JC, McLauchlan WR, Juge N (2000) High-level production of recombinant fungal endo-beta-1,4-xylanases in the methylotrophic yeast Pichia pastoris. Protein Expr Purif 19:179-187
    • (2000) Protein Expr Purif , vol.19 , pp. 179-187
    • Berrin, J.G.1    Williamson, G.2    Puigserver, A.3    Chaix, J.C.4    McLauchlan, W.R.5    Juge, N.6
  • 2
    • 34548031229 scopus 로고    scopus 로고
    • Cloning, expression and enzyme characterization analysis of Aspergillus sulphureus xylanase gene xynA
    • Cao YH, Chen XL, He PL, Lu WQ (2006) Cloning, expression and enzyme characterization analysis of Aspergillus sulphureus xylanase gene xynA. Lett Biotechnol 17:858-861
    • (2006) Lett Biotechnol , vol.17 , pp. 858-861
    • Cao, Y.H.1    Chen, X.L.2    He, P.L.3    Lu, W.Q.4
  • 3
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T, Gerday C, Feller G (2005) Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol Rev 29:3-23
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 4
    • 0016906505 scopus 로고
    • Hemicellulases: Their occurrence, purification, properties and mode of action
    • Dekker RFH, Richards GN (1976) Hemicellulases: their occurrence, purification, properties and mode of action. Adv Carbohydr Chem Biochem 32:277-352
    • (1976) Adv Carbohydr Chem Biochem , vol.32 , pp. 277-352
    • Dekker, R.F.H.1    Richards, G.N.2
  • 5
    • 33745961179 scopus 로고    scopus 로고
    • Cloning of a gene encoding an acidophilic endo-β-1,4-xylanase obtained from Aspergillus niger CGMCC1067 and constitutive expression in Pichia pastoris
    • Deng P, Li DF, Cao YH, Lu WQ, Wang CL (2006) Cloning of a gene encoding an acidophilic endo-β-1,4-xylanase obtained from Aspergillus niger CGMCC1067 and constitutive expression in Pichia pastoris. Enzyme Microb Technol 39:1096-1102
    • (2006) Enzyme Microb Technol , vol.39 , pp. 1096-1102
    • Deng, P.1    Li, D.F.2    Cao, Y.H.3    Lu, W.Q.4    Wang, C.L.5
  • 6
    • 0345647574 scopus 로고
    • Purification and some properties of xylanase from Penicillium herquei Bainier and Sartory
    • Funaguma T, Naito S, Morita M, Okumara M, Sugiura M, Hara A (1991) Purification and some properties of xylanase from Penicillium herquei Bainier and Sartory. Agric Biol Chem 55:1163-1165
    • (1991) Agric Biol Chem , vol.55 , pp. 1163-1165
    • Funaguma, T.1    Naito, S.2    Morita, M.3    Okumara, M.4    Sugiura, M.5    Hara, A.6
  • 7
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280:309-316
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 8
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293:781-788
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 9
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B, Davies G (1997) Structural and sequence-based classification of glycoside hydrolases. Curr Opin Struct Biol 7:637-644
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 10
    • 0031424642 scopus 로고    scopus 로고
    • High-level expression of bovine β-lactoglobulin in Pichia pastoris and characterization of its physical properties
    • Kim TR, Goto Y, Hirota N, Dawata K, Denton H, Wu SY, Sawyer L, Batt CA (1997) High-level expression of bovine β-lactoglobulin in Pichia pastoris and characterization of its physical properties. Protein Eng 10:1339-1345
    • (1997) Protein Eng , vol.10 , pp. 1339-1345
    • Kim, T.R.1    Goto, Y.2    Hirota, N.3    Dawata, K.4    Denton, H.5    Wu, S.Y.6    Sawyer, L.7    Batt, C.A.8
  • 11
    • 0037780133 scopus 로고    scopus 로고
    • First crystallographic structure of a xylanase from glycoside hydrolase family 5: Implications for catalysis
    • Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A (2003) First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis. Biochemistry 42:8411-8422
    • (2003) Biochemistry , vol.42 , pp. 8411-8422
    • Larson, S.B.1    Day, J.2    Barba De La Rosa, A.P.3    Keen, N.T.4    McPherson, A.5
  • 12
    • 0037415354 scopus 로고    scopus 로고
    • Influence of water activity and temperature on xylanase biosynthesis in pilot-scale solid-state fermentation by Aspergillus sulphureus
    • Lu WQ, Li DF, Wu YB (2003) Influence of water activity and temperature on xylanase biosynthesis in pilot-scale solid-state fermentation by Aspergillus sulphureus. Enzyme Microb Technol 32:305-311
    • (2003) Enzyme Microb Technol , vol.32 , pp. 305-311
    • Lu, W.Q.1    Li, D.F.2    Wu, Y.B.3
  • 14
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal Chem 31:426-428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 15
    • 0027968572 scopus 로고
    • Identification of two acidic residues involved in the catalysis of xylanase a from Streptomyces lividans
    • Moreau A, Roberge M, Manin C, Shareck F, Kluepfel D, Morosoli R (1994) Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans. Biochem J 302:291-295
    • (1994) Biochem J , vol.302 , pp. 291-295
    • Moreau, A.1    Roberge, M.2    Manin, C.3    Shareck, F.4    Kluepfel, D.5    Morosoli, R.6
  • 16
    • 0032488932 scopus 로고    scopus 로고
    • Overexpression of human procarboxypeptidase A2 in Pichia pastoris and detailed characterization of its activation pathway
    • Reverter D, Ventura S, Villegas V, Vendrell J, Avilés FX (1998) Overexpression of human procarboxypeptidase A2 in Pichia pastoris and detailed characterization of its activation pathway. J Biol Chem 273:3535-3541
    • (1998) J Biol Chem , vol.273 , pp. 3535-3541
    • Reverter, D.1    Ventura, S.2    Villegas, V.3    Vendrell, J.4    Avilés, F.X.5
  • 17
    • 0022856787 scopus 로고
    • An evolutionary perspective on synonymous codon usage in unicellular organisms
    • Sharp PM, Li WH (1986) An evolutionary perspective on synonymous codon usage in unicellular organisms. J Mol Evol 24:28-38
    • (1986) J Mol Evol , vol.24 , pp. 28-38
    • Sharp, P.M.1    Li, W.H.2
  • 18
    • 0030642144 scopus 로고    scopus 로고
    • Xylanolytic enzymes from fungi and bacteria
    • Sunna A, Antranikian G (1997) Xylanolytic enzymes from fungi and bacteria. Crit Rev Biotechnol 17:39-67
    • (1997) Crit Rev Biotechnol , vol.17 , pp. 39-67
    • Sunna, A.1    Antranikian, G.2
  • 19
    • 0031579445 scopus 로고    scopus 로고
    • Isolation of the Pichia pastoris glyceraldehydes-3-phosphate dehydrogenase gene and regulation and use of its promoter
    • Waterham HR, Digan ME, Koutz PJ, Lair SV, Cregg JM (1997) Isolation of the Pichia pastoris glyceraldehydes-3-phosphate dehydrogenase gene and regulation and use of its promoter. Gene 186:37-44
    • (1997) Gene , vol.186 , pp. 37-44
    • Waterham, H.R.1    Digan, M.E.2    Koutz, P.J.3    Lair, S.V.4    Cregg, J.M.5
  • 20
    • 0024087074 scopus 로고
    • Multiplicity of β-1,4-xylanase in microorganisms: Function and applicants
    • Wong KKY, Tan LUL, Saddler JN (1988) Multiplicity of β-1,4-xylanase in microorganisms: function and applicants. Microbiol Rev 52:305-317
    • (1988) Microbiol Rev , vol.52 , pp. 305-317
    • Wong, K.K.Y.1    Tan, L.U.L.2    Saddler, J.N.3
  • 22
    • 0034182261 scopus 로고    scopus 로고
    • Synonymous codon usage in Pichia pastoris
    • Zhao X, Huo KK, Li YY (2000) Synonymous codon usage in Pichia pastoris. Chin J Biotechnol 16:308-311
    • (2000) Chin J Biotechnol , vol.16 , pp. 308-311
    • Zhao, X.1    Huo, K.K.2    Li, Y.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.