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Volumn 66, Issue 6, 2000, Pages 2438-2444

Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic antarctic Planococcus isolate

Author keywords

[No Author keywords available]

Indexed keywords

ANTARCTICA; ARTICLE; BACTERIUM IDENTIFICATION; ENZYME PURIFICATION; GRAM POSITIVE BACTERIUM; MOLECULAR CLONING; MORPHOLOGY; NONHUMAN; NUCLEOTIDE SEQUENCE; PLANOCOCCUS; POND; SEQUENCE ANALYSIS;

EID: 0034080264     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.6.2438-2444.2000     Document Type: Article
Times cited : (87)

References (30)
  • 2
    • 0030513148 scopus 로고    scopus 로고
    • Psychrophilic microorganisms and their cold-active enzymes
    • Brenchley, J. 1996. Psychrophilic microorganisms and their cold-active enzymes. J. Ind. Microbiol. 17:432-437.
    • (1996) J. Ind. Microbiol. , vol.17 , pp. 432-437
    • Brenchley, J.1
  • 3
    • 0032729449 scopus 로고    scopus 로고
    • Biochemical and phylogenetic analyses of a cold-active β-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA
    • Coombs, J. M., and J. E. Brenchley. 1999. Biochemical and phylogenetic analyses of a cold-active β-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA. Appl. Environ. Microbiol. 65:5443-5450.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5443-5450
    • Coombs, J.M.1    Brenchley, J.E.2
  • 4
    • 0030937787 scopus 로고    scopus 로고
    • Active-site motifs of lysosomal acid hydrolases: Invariant features of clan GH-A glycosyl hydrolases deduced from hydrophobic cluster analysis
    • Durand, P., P. Lehn, I. Callebaut, S. Fabrega, B. Henrissat, and J.-P. Mornon. 1997. Active-site motifs of lysosomal acid hydrolases: invariant features of clan GH-A glycosyl hydrolases deduced from hydrophobic cluster analysis. Glycobiology 7:277-284.
    • (1997) Glycobiology , vol.7 , pp. 277-284
    • Durand, P.1    Lehn, P.2    Callebaut, I.3    Fabrega, S.4    Henrissat, B.5    Mornon, J.-P.6
  • 6
    • 0025804758 scopus 로고
    • Domains in microbial β-1,4-glycanases: Sequence conservation, function, and enzyme families
    • Gilkes, N. R., B. Henrissat, D. G. Kilburn, R. C. Miller, Jr., and R. A. J. Warren. 1991. Domains in microbial β-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol. Rev. 55:303-315.
    • (1991) Microbiol. Rev. , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller R.C., Jr.4    Warren, R.A.J.5
  • 7
    • 0025322547 scopus 로고
    • Tangential flow filtration and preliminary phylogenetic analysis of marine picoplankton
    • Giovannoni, S. J., E. F. DeLong, T. M. Schmidt, and N. R. Pace. 1990. Tangential flow filtration and preliminary phylogenetic analysis of marine picoplankton. Appl. Environ. Microbiol. 56:2572-2575.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2572-2575
    • Giovannoni, S.J.1    DeLong, E.F.2    Schmidt, T.M.3    Pace, N.R.4
  • 8
    • 0028913174 scopus 로고
    • Analysis of a novel gene and β-galactosidase isozyme from a psychrotrophic Arthrobacter isolate
    • Gutshall, K. R., D. E. Trimbur, J. J. Kasmir, and J. E. Brenchley. 1995. Analysis of a novel gene and β-galactosidase isozyme from a psychrotrophic Arthrobacter isolate. J. Bacteriol. 177:1981-1988.
    • (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
    • 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
  • 10
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and A. Bairoch. 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
  • 11
    • 0022641866 scopus 로고
    • Structure of a β-galactosidase gene of Bacillus stearothermophilus
    • Hirata, H., T. Fukazawa, S. Negoro, and H. Okada. 1986. Structure of a β-galactosidase gene of Bacillus stearothermophilus. J. Bacteriol. 166:722-727.
    • (1986) J. Bacteriol. , vol.166 , pp. 722-727
    • Hirata, H.1    Fukazawa, T.2    Negoro, S.3    Okada, H.4
  • 13
    • 0031854020 scopus 로고    scopus 로고
    • Arthrobacter, Brachybacterium and Planococcus isolates identified from Antarctic sea ice brine. Description of Planococcus mcmeekinii, sp. nov.
    • Junge, K., J. J. Gosink, H. G. Hoppe, and J. T. Staley. 1998. Arthrobacter, Brachybacterium and Planococcus isolates identified from Antarctic sea ice brine. Description of Planococcus mcmeekinii, sp. nov. Syst. Appl. Microbiol. 21:306-314.
    • (1998) Syst. Appl. Microbiol. , vol.21 , pp. 306-314
    • Junge, K.1    Gosink, J.J.2    Hoppe, H.G.3    Staley, J.T.4
  • 14
  • 15
    • 0032980515 scopus 로고    scopus 로고
    • Biochemical and phylogenetic analyses of psychrophilic isolates belonging to the Arthrobacter subgroup and description of Arthrobacter psychrolactophilus, sp. nov.
    • Loveland-Curtze, J., P. P. Sheridan, K. R. Gutshall, and J. E. Brenchley. 1999. Biochemical and phylogenetic analyses of psychrophilic isolates belonging to the Arthrobacter subgroup and description of Arthrobacter psychrolactophilus, sp. nov. Arch. Microbiol. 177:355-363.
    • (1999) Arch. Microbiol. , vol.177 , pp. 355-363
    • Loveland-Curtze, J.1    Sheridan, P.P.2    Gutshall, K.R.3    Brenchley, J.E.4
  • 17
  • 18
    • 0031178553 scopus 로고    scopus 로고
    • Galactosyl transfer onto p-nitrophenyl β-D-glucosidase using β-D-galactosidase from Bacillus circulans
    • Murata, T., S. Akimoto, M. Horimoto, and T. Usui. 1997. Galactosyl transfer onto p-nitrophenyl β-D-glucosidase using β-D-galactosidase from Bacillus circulans. Biosci. Biotechnol. Biochem. 61:1118-1120.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1118-1120
    • Murata, T.1    Akimoto, S.2    Horimoto, M.3    Usui, T.4
  • 19
    • 0032135068 scopus 로고    scopus 로고
    • Thermostable β-galactosidase from an extreme thermophile, Thermos sp. A4: Enzyme purification and characterization, and gene cloning and sequencing
    • Ohtsu, N., H. Motoshima, K. Goto, F. Tsukasaki, and H. Matsuzawa. 1998. Thermostable β-galactosidase from an extreme thermophile, Thermos sp. A4: enzyme purification and characterization, and gene cloning and sequencing. Biosci. Biotechnol. Biochem. 62:1539-1545.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1539-1545
    • Ohtsu, N.1    Motoshima, H.2    Goto, K.3    Tsukasaki, F.4    Matsuzawa, H.5
  • 20
    • 0002842298 scopus 로고
    • The analysis of natural microbial populations by ribosomal RNA sequences
    • Pace, N. R., D. A. Stahl, D. J. Lane, and G. J. Olsen. 1986. The analysis of natural microbial populations by ribosomal RNA sequences. Adv. Microb. Ecol. 9:1-55.
    • (1986) Adv. Microb. Ecol. , vol.9 , pp. 1-55
    • Pace, N.R.1    Stahl, D.A.2    Lane, D.J.3    Olsen, G.J.4
  • 21
    • 0342275191 scopus 로고    scopus 로고
    • Optimisation of the BgaB reporter system: Determination of transcriptional regulation of stress responsive genes in Bacillus subtilis
    • Schrogel, O., and R. Allmansberger. 1997. Optimisation of the BgaB reporter system: determination of transcriptional regulation of stress responsive genes in Bacillus subtilis. FEMS Microbiol. Lett. 153:237-243.
    • (1997) FEMS Microbiol. Lett. , vol.153 , pp. 237-243
    • Schrogel, O.1    Allmansberger, R.2
  • 22
    • 0029147849 scopus 로고
    • Sequence analysis of flanking regions of the pfoA gene of Clostridium perfringens: β-galactosidase gene (pbg) is located in the 3′-flanking region
    • Shimizu, T., T. Kobayashi, W. Ba-Thein, K. Ohtani, and H. Hayashi. 1995. Sequence analysis of flanking regions of the pfoA gene of Clostridium perfringens: β-galactosidase gene (pbg) is located in the 3′-flanking region. Microbiol. Immunol. 39:677-686.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 677-686
    • Shimizu, T.1    Kobayashi, T.2    Ba-Thein, W.3    Ohtani, K.4    Hayashi, H.5
  • 25
    • 2642656325 scopus 로고    scopus 로고
    • Isolation of a β-galactosidase-encoding gene from Bacillus licheniformis: Purification and characterization of the recombinant enzyme expressed in Escherichia coli
    • Tran, L. P., L. Szabo, L. Fulop, L. Orosz, T. Sik, and A. Holczinger. 1998. Isolation of a β-galactosidase-encoding gene from Bacillus licheniformis: purification and characterization of the recombinant enzyme expressed in Escherichia coli. Curr. Microbiol. 37:39-43.
    • (1998) Curr. Microbiol. , vol.37 , pp. 39-43
    • Tran, L.P.1    Szabo, L.2    Fulop, L.3    Orosz, L.4    Sik, T.5    Holczinger, A.6
  • 26
    • 0028117834 scopus 로고
    • Characterization of a psychrotrophic Arthrobacter gene and its cold-active β-galactosidase
    • Trimbur, D. E., K. R. Gutshall, P. Prema, and J. E. Brenchley. 1994. Characterization of a psychrotrophic Arthrobacter gene and its cold-active β-galactosidase. Appl. Environ. Microbiol. 60:4544-4552.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4544-4552
    • Trimbur, D.E.1    Gutshall, K.R.2    Prema, P.3    Brenchley, J.E.4
  • 27
    • 0031777568 scopus 로고    scopus 로고
    • Structure of the β-galactosidase gene from Thermus sp. strain T2: Expression in Escherichia coli and purification in a single step of an active fusion protein
    • Vian, A., A. V. Carrascosa, J. L. Garcia, and E. Cortes. 1998. Structure of the β-galactosidase gene from Thermus sp. strain T2: expression in Escherichia coli and purification in a single step of an active fusion protein. Appl. Environ. Microbiol. 64:2187-2191.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2187-2191
    • Vian, A.1    Carrascosa, A.V.2    Garcia, J.L.3    Cortes, E.4
  • 28
  • 29
    • 0025206677 scopus 로고
    • New and future uses of enzymes in food processing
    • Whitaker, J. R. 1990. New and future uses of enzymes in food processing. Food Biotechnol. 4:669-697.
    • (1990) Food Biotechnol. , vol.4 , pp. 669-697
    • Whitaker, J.R.1
  • 30
    • 0032150597 scopus 로고    scopus 로고
    • Structures of novel acidic galactooligosaccharides synthesized by Bacillus circulans β-galactosidase
    • Yanahira, S., Y. Yabe, M. Nakakoshi, S. Miura, N. Matsubara, and H. Ishikawa. 1998. Structures of novel acidic galactooligosaccharides synthesized by Bacillus circulans β-galactosidase. Biosci. Biotechnol. Biochem. 62: 1791-1794.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1791-1794
    • Yanahira, S.1    Yabe, Y.2    Nakakoshi, M.3    Miura, S.4    Matsubara, N.5    Ishikawa, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.