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Volumn 66, Issue 2, 2000, Pages 788-793

Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CELLULASE; ENZYME VARIANT; GLUCOSE; HYBRID PROTEIN; HYDROLASE; MUTANT PROTEIN;

EID: 0033961548     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.2.788-793.2000     Document Type: Article
Times cited : (98)

References (30)
  • 1
    • 0031935580 scopus 로고    scopus 로고
    • Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
    • Asanuma, S., A. Yamagishi, N. Tanaka, and T. Oshima. 1998. Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Protein Sci. 7:698-705.
    • (1998) Protein Sci. , vol.7 , pp. 698-705
    • Asanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 3
    • 0012750361 scopus 로고
    • Industrial enzymes
    • V. Moses and R. E. Cape (ed.). Harwood Academic Publishers, Chur, Switzerland
    • Cowan, D. A. 1991. Industrial enzymes, p. 311-340 In V. Moses and R. E. Cape (ed.), Biotechnology: the science and the business - 1991. Harwood Academic Publishers, Chur, Switzerland.
    • (1991) Biotechnology: the Science and the Business - 1991 , pp. 311-340
    • Cowan, D.A.1
  • 4
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou, G., C. Stathopoulos, P. S. Daugherty, A. R. Nayak, B. L. Iverson, and R. Curtiss III. 1997. Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat. Biotechnol. 15:29-34.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5    Curtiss R. III6
  • 5
    • 0032085975 scopus 로고    scopus 로고
    • Combinatorial protein design by in vitro recombination
    • Giver, L., and F. H. Arnold. 1998. Combinatorial protein design by in vitro recombination. Curr. Opin. Chem. Biol. 2:335-338.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 335-338
    • Giver, L.1    Arnold, F.H.2
  • 6
    • 3242793191 scopus 로고
    • Direct clone characterization from plaques and colonies by the polymerase chain reaction
    • Gussow, D., and T. Clackson. 1989. Direct clone characterization from plaques and colonies by the polymerase chain reaction. Nucleic Acids Res. 17:4000.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4000
    • Gussow, D.1    Clackson, T.2
  • 7
    • 0000521463 scopus 로고
    • Characterization of a bifunctional cellulase and its structural gene: The cel gene of Bacillus sp. D04 has exo- and endoglucanase activity
    • Han, S. J., Y. J. Yoo, and H. S. Kang. 1995. Characterization of a bifunctional cellulase and its structural gene: the cel gene of Bacillus sp. D04 has exo- and endoglucanase activity. J. Biol. Chem. 270:26012-26019.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26012-26019
    • Han, S.J.1    Yoo, Y.J.2    Kang, H.S.3
  • 8
    • 0032007562 scopus 로고    scopus 로고
    • Artificial evolution by DNA shuffling
    • Harayama, S. 1998. Artificial evolution by DNA shuffling. Trends Biotechnol. 16:76-82.
    • (1998) Trends Biotechnol. , vol.16 , pp. 76-82
    • Harayama, S.1
  • 9
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., H. Jojima, and H. Okajama. 1990. High efficiency transformation of Escherichia coli with plasmids. Gene 96:23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Jojima, H.2    Okajama, H.3
  • 10
    • 0031863713 scopus 로고    scopus 로고
    • Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae
    • Jung, H. C., J. M. Lebeault, and J. G. Pan. 1998. Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae. Nat. Biotechnol. 16:576-580.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 576-580
    • Jung, H.C.1    Lebeault, J.M.2    Pan, J.G.3
  • 11
    • 0032055018 scopus 로고    scopus 로고
    • Expression of carboxymethylcellulase on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein
    • Jung, H. C., J. H. Park, S. H. Park, J. M. Lebeault, and J. G. Pan. 1998. Expression of carboxymethylcellulase on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein. Enzyme Microb. Technol. 22: 348-354.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 348-354
    • Jung, H.C.1    Park, J.H.2    Park, S.H.3    Lebeault, J.M.4    Pan, J.G.5
  • 12
    • 0030864556 scopus 로고    scopus 로고
    • 3D structural information as a guide to protein engineering using genetic selection
    • Kast, P., and D. Hilvert. 1997. 3D structural information as a guide to protein engineering using genetic selection. Curr. Opin. Struct. Biol. 7:470-479.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 470-479
    • Kast, P.1    Hilvert, D.2
  • 13
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner, O., and F. H. Arnold. 1997. Directed evolution of enzyme catalysts. Trends Biotechnol. 15:523-530.
    • (1997) Trends Biotechnol. , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 14
    • 0032549781 scopus 로고    scopus 로고
    • Redesigning enzyme topology by directed evolution
    • MacBeath, G., P. Kast, and D. Hilvert. 1998. Redesigning enzyme topology by directed evolution. Science 279:1958-1961.
    • (1998) Science , vol.279 , pp. 1958-1961
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 15
    • 0345367460 scopus 로고    scopus 로고
    • Quantitative assay system for specific enzyme activity using antibody: The case of protease, subtilisin BPN′
    • Miyota, Y., S. Komada, H. Momose, and S. Taguchi. 1998. Quantitative assay system for specific enzyme activity using antibody: the case of protease, subtilisin BPN′. J. Biotechnol. 66:157-163.
    • (1998) J. Biotechnol. , vol.66 , pp. 157-163
    • Miyota, Y.1    Komada, S.2    Momose, H.3    Taguchi, S.4
  • 16
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • Moore, J. C., and F. H. Arnold. 1996. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat. Biotechnol. 14:458-467.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 17
    • 0031921553 scopus 로고    scopus 로고
    • Selection of a subtilisin-hyperproducing Bacillus in a highly structured environment
    • Naki, D., C. Paech, G. Ganshaw, and V. Schellenberger. 1998. Selection of a subtilisin-hyperproducing Bacillus in a highly structured environment. Appl. Microbiol. Biotechnol. 49:290-294.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 290-294
    • Naki, D.1    Paech, C.2    Ganshaw, G.3    Schellenberger, V.4
  • 19
    • 0026110332 scopus 로고
    • Characterization and structure of the cellulase gene of Bacillus subtilis BSE616
    • Park, S. H., H. K. Kim, and M. Y. Pack. 1991. Characterization and structure of the cellulase gene of Bacillus subtilis BSE616. Agric. Biol. Chem. 55:441-448.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 441-448
    • Park, S.H.1    Kim, H.K.2    Pack, M.Y.3
  • 20
    • 0022908581 scopus 로고
    • Cloning and expression of a Bacillus cellulase gene in Escherichia coli
    • Park, S. H., and M. Y. Pack. 1986. Cloning and expression of a Bacillus cellulase gene in Escherichia coli. Enzyme Microb. Technol. 8:725-728.
    • (1986) Enzyme Microb. Technol. , vol.8 , pp. 725-728
    • Park, S.H.1    Pack, M.Y.2
  • 21
    • 0031442821 scopus 로고    scopus 로고
    • Creating novel enzymes by applied molecular evolution
    • Skandalis, A., L. P. Encell, and L. A. Loeb. 1997. Creating novel enzymes by applied molecular evolution. Chem. Biol. 4:889-898.
    • (1997) Chem. Biol. , vol.4 , pp. 889-898
    • Skandalis, A.1    Encell, L.P.2    Loeb, L.A.3
  • 23
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. 1994. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370:389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 25
    • 0029927067 scopus 로고    scopus 로고
    • Phage display of proteases and macromolecular inhibitors
    • Wang, C. I., Q. Yang, and C. S. Craik 1996. Phage display of proteases and macromolecular inhibitors. Methods Enzymol. 267:52-68.
    • (1996) Methods Enzymol. , vol.267 , pp. 52-68
    • Wang, C.I.1    Yang, Q.2    Craik, C.S.3
  • 26
    • 0002499398 scopus 로고
    • Use of complex formation between Congo red and polysaccharides in detection and assay of polysaccharide hydrolases
    • Wood, P. J., J. D. Erfle, and R. M. Teather. 1988. Use of complex formation between Congo red and polysaccharides in detection and assay of polysaccharide hydrolases. Methods Enzymol. 60:59-74.
    • (1988) Methods Enzymol. , vol.60 , pp. 59-74
    • Wood, P.J.1    Erfle, J.D.2    Teather, R.M.3
  • 27
    • 0032510667 scopus 로고    scopus 로고
    • Directed evolution of an aspartate aminotransferase with new substrate specificities
    • Yano, T., S. Oue, and H. Kagamiyama. 1998. Directed evolution of an aspartate aminotransferase with new substrate specificities. Proc. Natl. Acad. Sci. USA 95:5511-5515.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5511-5515
    • Yano, T.1    Oue, S.2    Kagamiyama, H.3
  • 28
    • 0033555718 scopus 로고    scopus 로고
    • The effect of high-frequency random mutagenesis on in vitro protein evolution: A study on TEM-1 beta-lactamase
    • Zaccolo, M., and E. Gherardi. 1999. The effect of high-frequency random mutagenesis on in vitro protein evolution: a study on TEM-1 beta-lactamase. J. Mol. Biol. 285:775-783.
    • (1999) J. Mol. Biol. , vol.285 , pp. 775-783
    • Zaccolo, M.1    Gherardi, E.2
  • 29
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang, J. H., G. Dawes, and W. P. Stemmer. 1997. Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA 94:4504-4509.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.H.1    Dawes, G.2    Stemmer, W.P.3
  • 30
    • 0030754926 scopus 로고    scopus 로고
    • Optimization of DNA shuffling for high fidelity recombination
    • Zhao, H., and F. H. Arnold. 1997. Optimization of DNA shuffling for high fidelity recombination. Nucleic Acids Res. 25:1307-1308.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1307-1308
    • Zhao, H.1    Arnold, F.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.