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Volumn 39, Issue 1, 2005, Pages 27-34

Cloning, expression, and purification of a recombinant cold-adapted β-galactosidase from antarctic bacterium Pseudoalteromonas sp. 22b

Author keywords

Cold adapted galactosidase; Lactose hydrolysis; Pseudoalteromonas sp.; Psychrotrophic microorganisms

Indexed keywords

BETA GALACTOSIDASE;

EID: 10644257663     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.09.002     Document Type: Article
Times cited : (73)

References (21)
  • 2
    • 0141645664 scopus 로고    scopus 로고
    • Cold-adapted enzymes
    • C.J. Marshall Cold-adapted enzymes TIBTECH 15 1997 358 359
    • (1997) TIBTECH , vol.15 , pp. 358-359
    • Marshall, C.J.1
  • 3
    • 0034170458 scopus 로고    scopus 로고
    • Towards a molecular understanding of cold activity of enzymes from psychrophiles
    • N.J. Russell Towards a molecular understanding of cold activity of enzymes from psychrophiles Extremophiles 4 2000 83 90
    • (2000) Extremophiles , vol.4 , pp. 83-90
    • Russell, N.J.1
  • 4
    • 0028314161 scopus 로고
    • Properties of cold-adapted microorganisms and their potential role in biotechnology
    • R. Margesin, and F. Schinner Properties of cold-adapted microorganisms and their potential role in biotechnology J. Biotechnol. 33 1994 1 14
    • (1994) J. Biotechnol. , vol.33 , pp. 1-14
    • Margesin, R.1    Schinner, F.2
  • 5
    • 0034159939 scopus 로고    scopus 로고
    • Cold-adapted enzymes: From fundamentals to biotechnology
    • C. Gerday, and G. Feller Cold-adapted enzymes: from fundamentals to biotechnology TIBTECH 18 2000 103 107
    • (2000) TIBTECH , vol.18 , pp. 103-107
    • Gerday, C.1    Feller, G.2
  • 6
    • 0028117834 scopus 로고
    • Characterization of a psychrotrophic Arthrobacter gene and its cold-active β-galactosidase
    • D.E. Trimbur, K.R. Gutshall, P. Prema, and J.E. Brenchley Characterization of a psychrotrophic Arthrobacter gene and its cold-active β-galactosidase Appl. Environ. Microbiol. 60 1994 4544 4552
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4544-4552
    • Trimbur, D.E.1    Gutshall, K.R.2    Prema, P.3    Brenchley, J.E.4
  • 7
    • 0030971550 scopus 로고    scopus 로고
    • A novel Arthrobacter β-galactosidase with homology to eukaryotic β-galactosidases
    • K.R. Gutshall, K. Wang, and J.E. Brenchley A novel Arthrobacter β-galactosidase with homology to eukaryotic β-galactosidases J. Bacteriol. 179 1997 3064 3067
    • (1997) J. Bacteriol. , vol.179 , pp. 3064-3067
    • Gutshall, K.R.1    Wang, K.2    Brenchley, J.E.3
  • 8
    • 0028913174 scopus 로고
    • Analysis of a novel gene and β-galactosidase isoenzyme from a psychrotrophic Arthrobacter isolate
    • K.R. Gutshall, D.E. Trimbur, J.J. Kasmir, and J.E. Brenchley Analysis of a novel gene and β-galactosidase isoenzyme from a psychrotrophic Arthrobacter isolate J. Bacteriol. 177 1995 1981 1988
    • (1995) J. Bacteriol. , vol.177 , pp. 1981-1988
    • Gutshall, K.R.1    Trimbur, D.E.2    Kasmir, J.J.3    Brenchley, J.E.4
  • 9
    • 0026176947 scopus 로고
    • Specificity, inhibitory studies, and oligosaccharide formation by β-galactosidase from psychrotrophic Bacillus subtilis KL88
    • K.A.A. Rahim, and B.H. Lee Specificity, inhibitory studies, and oligosaccharide formation by β-galactosidase from psychrotrophic Bacillus subtilis KL88 J. Dairy Sci. 74 1991 1773 1778
    • (1991) J. Dairy Sci. , vol.74 , pp. 1773-1778
    • Rahim, K.A.A.1    Lee, B.H.2
  • 10
    • 0032729449 scopus 로고    scopus 로고
    • Biochemical and phylogenetical analyses of a cold-active β-galactosidase from the lactic acid bacterium Carnobacterium piescicola BA
    • J.M. Coombs, and J.E. Brenchley Biochemical and phylogenetical analyses of a cold-active β-galactosidase from the lactic acid bacterium Carnobacterium piescicola BA Appl. Environ. Microbiol. 65 1999 5443 5450
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5443-5450
    • Coombs, J.M.1    Brenchley, J.E.2
  • 12
    • 0034080264 scopus 로고    scopus 로고
    • Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic Antarctic Planococcus isolate
    • P.P. Sheridan, and J.E. Brenchley Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic Antarctic Planococcus isolate Appl. Environ. Microbiol. 66 2000 2438 2444
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2438-2444
    • Sheridan, P.P.1    Brenchley, J.E.2
  • 13
    • 0043068040 scopus 로고    scopus 로고
    • Antarctic marine bacterium Pseudoalteromonas sp. 22b as a source of cold-adapted β-galactosidase
    • M. Turkiewicz, J. Kur, A. Bialkowska, H. Cieslinski, H. Kalinowska, and S. Bielecki Antarctic marine bacterium Pseudoalteromonas sp. 22b as a source of cold-adapted β-galactosidase Biomol. Eng. 20 2003 317 324
    • (2003) Biomol. Eng. , vol.20 , pp. 317-324
    • Turkiewicz, M.1    Kur, J.2    Bialkowska, A.3    Cieslinski, H.4    Kalinowska, H.5    Bielecki, S.6
  • 14
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • F.W. Studier, and B.A. Moffatt Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J. Mol. Biol. 189 1986 113 130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method fort he quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method fort he quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • B. Henrissat, and G. Davies Structural and sequence-based classification of glycoside hydrolases Curr. Opin. Struct. Biol. 7 1997 637 644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 18
    • 0025231773 scopus 로고
    • Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis
    • C.G. Cupples, J.H. Miller, and R.E. Huber Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis J. Biol. Chem. 265 1990 5512 5518
    • (1990) J. Biol. Chem. , vol.265 , pp. 5512-5518
    • Cupples, C.G.1    Miller, J.H.2    Huber, R.E.3
  • 19
    • 0026668499 scopus 로고
    • Glu-537, not Glu-461, is the nucleophile in the active site of (lacZ) β-galactosidase from Escherichia coli
    • J.C. Gebler, R. Aebersold, and S.G. Withers Glu-537, not Glu-461, is the nucleophile in the active site of (lacZ) β-galactosidase from Escherichia coli J. Biol. Chem. 267 1992 11126 11130
    • (1992) J. Biol. Chem. , vol.267 , pp. 11126-11130
    • Gebler, J.C.1    Aebersold, R.2    Withers, S.G.3
  • 20
    • 0020689671 scopus 로고
    • Sequence of the lacZ gene of Escherichia coli
    • A. Kalnins, K. Otto, U. Ruther, and B. Muller-Hill Sequence of the lacZ gene of Escherichia coli EMBO J. 2 1983 593 597
    • (1983) EMBO J. , vol.2 , pp. 593-597
    • Kalnins, A.1    Otto, K.2    Ruther, U.3    Muller-Hill, B.4
  • 21
    • 0028178377 scopus 로고
    • Three-dimensional structure of beta-galactosidase from E. coli
    • R.H. Jacobson, X.J. Zhang, R.F. DuBose, and B.W. Matthews Three-dimensional structure of beta-galactosidase from E. coli Nature 369 1994 761 766
    • (1994) Nature , vol.369 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2    Dubose, R.F.3    Matthews, B.W.4


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