메뉴 건너뛰기




Volumn 329, Issue 1-2, 2004, Pages 187-195

Molecular cloning and characterization of two thermostable carboxyl esterases from Geobacillus stearothermophilus

Author keywords

hydrolase; Bacillus; EDTA; Esterase; Ethylenediaminetetraacentate; Insertion sequence; IS; IS element; Kinetics; nt.; PAGE; PCR; Polyacrylamide gel electrophoresis; Polymerase chain reaction; Polyvinylidene difluoride; PVDF; SDS; Sodium dodecylsulphate

Indexed keywords

AMINO ACID; CARBOXYLESTERASE; ESTERASE; HEXANOIC ACID DERIVATIVE; POLYPEPTIDE; TRIACYLGLYCEROL LIPASE;

EID: 1642411072     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2003.12.029     Document Type: Article
Times cited : (92)

References (30)
  • 2
    • 0000076979 scopus 로고
    • Purification and properties of a thermostable esterase of Bacillus stearothermophilus produced by recombinant Bacillus brevis
    • Amaki Y., Tulin E.E., Ueda S., Ohmiya K., Yamane T. Purification and properties of a thermostable esterase of Bacillus stearothermophilus produced by recombinant Bacillus brevis. Biosci. Biotechnol. Biochem. 56:1992;238-241.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 238-241
    • Amaki, Y.1    Tulin, E.E.2    Ueda, S.3    Ohmiya, K.4    Yamane, T.5
  • 3
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • Arpigny J.L., Jaeger K.E. Bacterial lipolytic enzymes: classification and properties. Biochem. J. 343:1999;177-183.
    • (1999) Biochem. J. , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 5
    • 0031726827 scopus 로고    scopus 로고
    • Molecular analysis of a gene encoding a cell-bound esterase from Streptomyces chrysomallus
    • Berger R., Hoffmann M., Keller U. Molecular analysis of a gene encoding a cell-bound esterase from Streptomyces chrysomallus. J. Bacteriol. 180:1998;6396-6399.
    • (1998) J. Bacteriol. , vol.180 , pp. 6396-6399
    • Berger, R.1    Hoffmann, M.2    Keller, U.3
  • 7
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: Classification, properties and application in biocatalysis
    • Bornscheuer U.T. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol. Rev. 26:2002;78-81.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 78-81
    • Bornscheuer, U.T.1
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 7:1976;248-254.
    • (1976) Anal. Biochem. , vol.7 , pp. 248-254
    • Bradford, M.1
  • 9
    • 0024971021 scopus 로고
    • Stability and activity of thermostable malic enzyme in denaturants and water-miscible organic solvents
    • Guagliardi A., Manco G., Rossi M., Bartolucci S. Stability and activity of thermostable malic enzyme in denaturants and water-miscible organic solvents. Eur. J. Biochem. 183:1989;25-30.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 25-30
    • Guagliardi, A.1    Manco, G.2    Rossi, M.3    Bartolucci, S.4
  • 10
    • 0017057332 scopus 로고
    • Intracellular esterases of Bacillus subtilis
    • D. Schlessinger. Washington, D.C: American Society for Microbiology
    • Higerd T.B., Riefler J.F. III Intracellular esterases of Bacillus subtilis. Schlessinger D. Microbiology. 1976;202-206 American Society for Microbiology, Washington, D.C.
    • (1976) Microbiology , pp. 202-206
    • Higerd, T.B.1    Riefler III, J.F.2
  • 11
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones
    • Khalameyzer V., Fischer I., Bornscheuer U.T., Altenbuchner J. Screening, nucleotide sequence and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones. Appl. Environ. Microbiol. 65:1999;477-482.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 477-482
    • Khalameyzer, V.1    Fischer, I.2    Bornscheuer, U.T.3    Altenbuchner, J.4
  • 12
    • 0002452053 scopus 로고    scopus 로고
    • Purification and partial characterization of thermostable carboxylesterase from Bacillus stearothermophilus L1
    • Kim H., Park S., Oh T. Purification and partial characterization of thermostable carboxylesterase from Bacillus stearothermophilus L1. J. Microbiol. Biotechnol. 7:1997;37-42.
    • (1997) J. Microbiol. Biotechnol. , vol.7 , pp. 37-42
    • Kim, H.1    Park, S.2    Oh, T.3
  • 13
    • 0027025870 scopus 로고
    • Molecular cloning and structure of the gene for esterase from a thermophilic bacterium, Bacillus stearothermophilus IFO 12550
    • Kugimiya W., Otani Y., Hashimoto Y. Molecular cloning and structure of the gene for esterase from a thermophilic bacterium, Bacillus stearothermophilus IFO 12550. Biosci. Biotechnol. Biochem. 56:1992;2074-2075.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 2074-2075
    • Kugimiya, W.1    Otani, Y.2    Hashimoto, Y.3
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0041521070 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction data for carboxylesterase Est30 from Bacillus stearothermophilus
    • Liu P., Wang Y.F., Ewis H.E., Abdelal A.T., Lu C.D., Weber I.T. Crystallization and preliminary X-ray diffraction data for carboxylesterase Est30 from Bacillus stearothermophilus. Acta Crystallogr., D Biol. Crystallogr. 59(Pt. 8):2003;1472-1473.
    • (2003) Acta Crystallogr., D Biol. Crystallogr. , vol.59 , Issue.PT. 8 , pp. 1472-1473
    • Liu, P.1    Wang, Y.F.2    Ewis, H.E.3    Abdelal, A.T.4    Lu, C.D.5    Weber, I.T.6
  • 16
    • 0027588112 scopus 로고
    • Enzymes in the synthesis of chiral drugs
    • Margolin A.L. Enzymes in the synthesis of chiral drugs. Enzyme Microb. Technol. 15:1993;262-280.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 262-280
    • Margolin, A.L.1
  • 17
    • 0034566882 scopus 로고    scopus 로고
    • Isolation and characterization of lipid-degrading Bacillus thermoleovorans IHI-91 from an Icelandic hot spring
    • Markossian S., Becker P., Markl H., Antranikian G. Isolation and characterization of lipid-degrading Bacillus thermoleovorans IHI-91 from an Icelandic hot spring. Extremophiles. 4:2000;365-371.
    • (2000) Extremophiles , vol.4 , pp. 365-371
    • Markossian, S.1    Becker, P.2    Markl, H.3    Antranikian, G.4
  • 18
    • 0010527942 scopus 로고
    • Kinetic resolution of racemic β, γ-epoxy esters with pig liver esterase
    • Moher P., Rosslein L., Tamm C. Kinetic resolution of racemic β, γ-epoxy esters with pig liver esterase. Tetrahedron Lett. 30:1989;2513-2516.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 2513-2516
    • Moher, P.1    Rosslein, L.2    Tamm, C.3
  • 19
    • 0037160540 scopus 로고    scopus 로고
    • A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: Cloning of the gene, characterization of the protein
    • Morana A.D.P., Di Prizito N., Aurilia V., Rossi M., Cannio R. A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene, characterization of the protein. Gene. 283:2002;107-115.
    • (2002) Gene , vol.283 , pp. 107-115
    • Morana, A.D.P.1    Di Prizito, N.2    Aurilia, V.3    Rossi, M.4    Cannio, R.5
  • 20
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu H.C., Heppel L.A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240:1965;3685-3691.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3691
    • Neu, H.C.1    Heppel, L.A.2
  • 21
    • 0024726863 scopus 로고
    • Correlation between microbial protein thermostability and resistance to denaturation in aqueous: Organic solvent two-phase systems
    • Owsu R.K., Cowan D.A. Correlation between microbial protein thermostability and resistance to denaturation in aqueous: organic solvent two-phase systems. Enzyme Microb. Technol. 11:1989;568-574.
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 568-574
    • Owsu, R.K.1    Cowan, D.A.2
  • 22
    • 0035098789 scopus 로고    scopus 로고
    • Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7
    • Prim N., Javier P.F.L., Diaz P. Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7. Curr. Microbiol. 42:2001;237-240.
    • (2001) Curr. Microbiol. , vol.42 , pp. 237-240
    • Prim, N.1    Javier, P.F.L.2    Diaz, P.3
  • 23
    • 0028305905 scopus 로고
    • Development of a new Bacillus carboxyl esterase for use in the resolution of chiral drugs
    • Quax W.J., Broekhuizen C.P. Development of a new Bacillus carboxyl esterase for use in the resolution of chiral drugs. Appl. Microbiol. Biotechnol. 41:1994;425-431.
    • (1994) Appl. Microbiol. Biotechnol. , vol.41 , pp. 425-431
    • Quax, W.J.1    Broekhuizen, C.P.2
  • 24
    • 0011140369 scopus 로고
    • Molecular cloning: A laboratory manual
    • Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory Press
    • Sambrook J., Fritsch E.F., Maniatis T. Molecular cloning: a laboratory manual. 2nd ed. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1989) 2nd Ed.
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 25
    • 0033870741 scopus 로고    scopus 로고
    • The transposable elements IS4712 prevents S-layer gene (sbsA) expression in Bacillus stearothermophilus and also affects the synthesis of altered surface layer proteins
    • Scholz H., Hummel S., Witte A., Lubitz W., Kuen B. The transposable elements IS4712 prevents S-layer gene (sbsA) expression in Bacillus stearothermophilus and also affects the synthesis of altered surface layer proteins. Arch. Microbiol. 174:2000;97-103.
    • (2000) Arch. Microbiol. , vol.174 , pp. 97-103
    • Scholz, H.1    Hummel, S.2    Witte, A.3    Lubitz, W.4    Kuen, B.5
  • 27
    • 0032992213 scopus 로고    scopus 로고
    • Functional identification of the product of the Bacillus subtilis yvaL gene as a SecG homologue
    • Wely K.H.M., Swaving J., Broekhuizen C.P., Rose M., Quax W., Driessen A.J.M. Functional identification of the product of the Bacillus subtilis yvaL gene as a SecG homologue. J. Bacteriol. 181:1999;1786-1792.
    • (1999) J. Bacteriol. , vol.181 , pp. 1786-1792
    • Wely, K.H.M.1    Swaving, J.2    Broekhuizen, C.P.3    Rose, M.4    Quax, W.5    Driessen, A.J.M.6
  • 28
    • 0029073537 scopus 로고
    • Purification and partial characterization of a novel thermophilic carboxylesterase with high mesophilic specific activity
    • Wood A.N.P., Fernandez-Lafuente R., Cowan D.A. Purification and partial characterization of a novel thermophilic carboxylesterase with high mesophilic specific activity. Enzyme Microb. Technol. 17:1995;816-825.
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 816-825
    • Wood, A.N.P.1    Fernandez-Lafuente, R.2    Cowan, D.A.3
  • 29
    • 0030714615 scopus 로고    scopus 로고
    • Cloning and characterization of the arginine-specific carbamoyl-phophate synthase from Bacillus stearothermophilus
    • Yang H., Park S.M., Nolan W.C., Lu C.D., Abdelal A.T. Cloning and characterization of the arginine-specific carbamoyl-phophate synthase from Bacillus stearothermophilus. Eur. J. Biochem. 249:1997;443-449.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 443-449
    • Yang, H.1    Park, S.M.2    Nolan, W.C.3    Lu, C.D.4    Abdelal, A.T.5
  • 30
    • 0028567726 scopus 로고
    • The Bacillus subtilis pnbA gene encoding p-nitro phenyl esterase: Cloning, sequencing and high-level expression in Escherichia coli
    • Zock J., Cantwell C., Swartling J., Roland H., Pohl T., Sutton K., Rosteck P. Jr., McGilvray D., Queener S. The Bacillus subtilis pnbA gene encoding p-nitro phenyl esterase: cloning, sequencing and high-level expression in Escherichia coli. Gene. 15:1994;37-43.
    • (1994) Gene , vol.15 , pp. 37-43
    • Zock, J.1    Cantwell, C.2    Swartling, J.3    Roland, H.4    Pohl, T.5    Sutton, K.6    Rosteck, P.Jr.7    McGilvray, D.8    Queener, S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.