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Volumn 46, Issue 1, 2008, Pages 100-107

Cloning and characterization of thermostable esterase from Archaeoglobus fulgidus

Author keywords

Archaeoglobus fulgidus; Enantioselectivity; Esterase; Extremophile; Thermostability

Indexed keywords

ARCHAEOGLOBUS FULGIDUS; ARCHAEOGLOBUS FULGIDUS DSM 4304; PSEUDOMONAS FLUORESCENS;

EID: 43249100626     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-007-0185-5     Document Type: Article
Times cited : (35)

References (26)
  • 2
    • 0037160540 scopus 로고    scopus 로고
    • A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: Cloning of the gene, characterization of the protein
    • Alessandra, M., D.P. Natascia, V. Aurilia, R. Mose, and C. Raffaele. 2002. A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene, characterization of the protein. Gene 283, 107-115.
    • (2002) Gene , vol.283 , pp. 107-115
    • Alessandra, M.1    Natascia, D.P.2    Aurilia, V.3    Mose, R.4    Raffaele, C.5
  • 3
    • 33751554235 scopus 로고
    • Chirality emerges as a key issues in pharmaceutical research
    • Borman, S. 1990. Chirality emerges as a key issues in pharmaceutical research. Chem. Eng. News 68, 9-14.
    • (1990) Chem. Eng. News , vol.68 , pp. 9-14
    • Borman, S.1
  • 4
    • 0032486517 scopus 로고    scopus 로고
    • Directed evolution of an esterase for the stereoselective resolution of a key intermediate in the synthesis of epothilones
    • Bornscheuer, U.T. 1997. Directed evolution of an esterase for the stereoselective resolution of a key intermediate in the synthesis of epothilones. Biotechnol. Bioeng. 58, 554-559.
    • (1997) Biotechnol. Bioeng. , vol.58 , pp. 554-559
    • Bornscheuer, U.T.1
  • 5
    • 0009877828 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: Classification, properties and application in biocatalysis
    • Bornscheuer, U.T. 2002. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol. Rev. 733, 1-9.
    • (2002) FEMS Microbiol. Rev. , vol.733 , pp. 1-9
    • Bornscheuer, U.T.1
  • 9
    • 1642411072 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two thermostable carboxyl esterase from Geobacillus stearothermophilus
    • Ewis, H.E., A.T. Abdelal, and C.-D. Lu. 2004. Molecular cloning and characterization of two thermostable carboxyl esterase from Geobacillus stearothermophilus. Gene 329, 187-195.
    • (2004) Gene , vol.329 , pp. 187-195
    • Ewis, H.E.1    Abdelal, A.T.2    Lu, C.-D.3
  • 10
    • 0027703508 scopus 로고
    • Prospects for the increase application of biocatalysts in organic transformations
    • Faber, K. and M.C.R. Franssen. 1993. Prospects for the increase application of biocatalysts in organic transformations. Trends Biotechnol. 11, 461-470.
    • (1993) Trends Biotechnol. , vol.11 , pp. 461-470
    • Faber, K.1    Franssen, M.C.R.2
  • 11
    • 0036251480 scopus 로고    scopus 로고
    • Biocatalytic preparation of enantiopure (R)-ketoprofen from its racemic ester by a new yeast isolate Citeromyces matriensis CGMCC 0573
    • Gong, P.-F., H.-Y. Wu, J.-H. Xu, D. Shen, and Y.-Y. Liu. 2002. Biocatalytic preparation of enantiopure (R)-ketoprofen from its racemic ester by a new yeast isolate Citeromyces matriensis CGMCC 0573. Appl. Microbiol. Biotechnol. 58, 728-734.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 728-734
    • Gong, P.-F.1    Wu, H.-Y.2    Xu, J.-H.3    Shen, D.4    Liu, Y.-Y.5
  • 12
    • 0037210701 scopus 로고    scopus 로고
    • Esterases from Bacillus subtilis and B. stearothermophilus share high sequence homology but differ substantially in their properties
    • Henke, E. and U.T. Bornscheuer. 2002. Esterases from Bacillus subtilis and B. stearothermophilus share high sequence homology but differ substantially in their properties. Appl. Microbiol. Biotechnol. 60, 320-326.
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 320-326
    • Henke, E.1    Bornscheuer, U.T.2
  • 13
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structure, and biotechnology applications of lipases
    • Jaeger, K.E., B.W. Dijkstra, and M.T. Reetz. 1999. Bacterial biocatalysts: molecular biology, three-dimensional structure, and biotechnology applications of lipases. Annu. Rev. Microbiol. 53, 315-351.
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 14
    • 0000088021 scopus 로고
    • Lipase catalysis and its application
    • Plenum press New York, NY, USA
    • John, V.T. and G. Abraham. 1991. Lipase catalysis and its application. In J.S. Dordick (ed.), Biocatalysts for industry. Plenum press, New York, NY, USA.
    • (1991) Biocatalysts for Industry
    • John, V.T.1    Abraham, G.2    Dordick, J.S.3
  • 15
    • 1242338176 scopus 로고    scopus 로고
    • Enhanced thermostability and tolerance of high substrate concentration of an esterase by directed evolution
    • Kim, J.-H., G.-S. Choi, S.-B. Kim, W.-H. Kim, J.-Y. Lee, Y.-W. Ryu, and G.-J. Kim. 2004. Enhanced thermostability and tolerance of high substrate concentration of an esterase by directed evolution. J. Mol. Catal. B: Enzymatic 27, 169-175.
    • (2004) J. Mol. Catal. B: Enzymatic , vol.27 , pp. 169-175
    • Kim, J.-H.1    Choi, G.-S.2    Kim, S.-B.3    Kim, W.-H.4    Lee, J.-Y.5    Ryu, Y.-W.6    Kim, G.-J.7
  • 16
    • 0035911359 scopus 로고    scopus 로고
    • Mapping the substrate selectivity of new hydrolases using colorimetric screening: Lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes
    • Liu, A.M.F., N.A. Somers, R.J. Kazlauskas, T.S. Brush, F. Zocher, M.M. Enzelberger, U.T. Bornscheuer, G.P. Horsman, A. Mezzetti, C. Schmidt-Dannert, and R.D. Schmid. 2001. Mapping the substrate selectivity of new hydrolases using colorimetric screening: lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes. Tetrahedron Asymmetry 12, 545-556.
    • (2001) Tetrahedron Asymmetry , vol.12 , pp. 545-556
    • Liu, A.M.F.1    Somers, N.A.2    Kazlauskas, R.J.3    Brush, T.S.4    Zocher, F.5    Enzelberger, M.M.6    Bornscheuer, U.T.7    Horsman, G.P.8    Mezzetti, A.9    Schmidt-Dannert, C.10    Schmid, R.D.11
  • 17
    • 0033958727 scopus 로고    scopus 로고
    • Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to Hormone-sensitive lipase subfamily from the Archaeon Archaeoglobus fulgidus
    • Manco, G., E. Giosue, S. D'Auria, P. Herman, G. Carrea, and M. Rossi. 2000. Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to Hormone-sensitive lipase subfamily from the Archaeon Archaeoglobus fulgidus. Arch. Biochem. Biophys. 373, 182-192.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 182-192
    • Manco, G.1    Giosue, E.2    D'Auria, S.3    Herman, P.4    Carrea, G.5    Rossi, M.6
  • 18
    • 0027588112 scopus 로고
    • Enzymes in the synthesis of chiral drugs
    • Margolin, A.L. 1993. Enzymes in the synthesis of chiral drugs. Enzyme Microb. Technol. 15, 266-280.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 266-280
    • Margolin, A.L.1
  • 23
    • 0036968065 scopus 로고    scopus 로고
    • Extremophiles: Developments of their special functions potential resources
    • Shinsuke, F. 2002. Extremophiles: Developments of their special functions potential resources. J. Biosci. Bioeng. 94, 518-525.
    • (2002) J. Biosci. Bioeng. , vol.94 , pp. 518-525
    • Shinsuke, F.1
  • 24
    • 0035681828 scopus 로고    scopus 로고
    • Conformational stability of a hyperthermophilic protein in various condition for denaturation
    • Shinsuke, F., S. Fujiwara, T. Imanaka, and M. Takagi. 2001. Conformational stability of a hyperthermophilic protein in various condition for denaturation. Electrochemistry 69, 949-952.
    • (2001) Electrochemistry , vol.69 , pp. 949-952
    • Shinsuke, F.1    Fujiwara, S.2    Imanaka, T.3    Takagi, M.4
  • 25
    • 0019836617 scopus 로고
    • Electrophoretic comparison of enzymes in the Gram-negative methanol-utilizing bacteria
    • Urakami, T. and K. Komagata. 1981. Electrophoretic comparison of enzymes in the Gram-negative methanol-utilizing bacteria. J. Gen. Appl. Microbiol. 27, 381-403.
    • (1981) J. Gen. Appl. Microbiol. , vol.27 , pp. 381-403
    • Urakami, T.1    Komagata, K.2
  • 26
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Source, uses, and molecular mechanism for thermostability
    • Vieille, C. and G.J. Zeikus. 2001. Hyperthermophilic enzymes: source, uses, and molecular mechanism for thermostability. Mol. Biol. Rev. 65, 1-43.
    • (2001) Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.