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Volumn 63, Issue 11, 1999, Pages 1865-1870

Characterization of a Thermostable Esterase Activity from the Moderate Thermophile Bacillus licheniformis

Author keywords

Bacillus licheniformis; Caproate; Esterase; Specificity

Indexed keywords

ESTERASE; RECOMBINANT PROTEIN;

EID: 0033217624     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1865     Document Type: Article
Times cited : (47)

References (31)
  • 1
    • 0023195109 scopus 로고
    • Isolation and characterisation of thermophilic bacterial strains with inulinase activity
    • Allais, J-J., Hoyos-Lopez, G., Kammoun, S., and Baratti, J., Isolation and characterisation of thermophilic bacterial strains with inulinase activity. Appi. Environ. Microbiol., 53, 942-945 (1987).
    • (1987) Appi. Environ. Microbiol. , vol.53 , pp. 942-945
    • Allais, J.-J.1    Hoyos-Lopez, G.2    Kammoun, S.3    Baratti, J.4
  • 2
    • 0031670591 scopus 로고    scopus 로고
    • Microbial growth and lipolytic activities of moderate thermophilic bacterial strains
    • Fakhreddine, L., Kademi, A., Ait-Abdelkader, N., and Baratti, J., Microbial growth and lipolytic activities of moderate thermophilic bacterial strains. Biotechnol. Letters, 20, 879-883 (1998).
    • (1998) Biotechnol. Letters , vol.20 , pp. 879-883
    • Fakhreddine, L.1    Kademi, A.2    Ait-Abdelkader, N.3    Baratti, J.4
  • 3
    • 0344572861 scopus 로고    scopus 로고
    • A thermostable esterase activity from newly isolated moderate thermophilic bacterial strains
    • Kademi, A., Ait-Abdelkader, N., Fakhreddine, L., and Baratti, J., A thermostable esterase activity from newly isolated moderate thermophilic bacterial strains. Enz. Microb. Technol., 24, 332-338 (1999).
    • (1999) Enz. Microb. Technol. , vol.24 , pp. 332-338
    • Kademi, A.1    Ait-Abdelkader, N.2    Fakhreddine, L.3    Baratti, J.4
  • 4
    • 85009624885 scopus 로고    scopus 로고
    • Properties of a thermostable esterase from the newly isolated moderate thermophilic bacterium Bacillus circulans
    • press
    • Kademi, A., Ait-Abdelkader, N., Fakhreddine, L., and Baratti, J., Properties of a thermostable esterase from the newly isolated moderate thermophilic bacterium Bacillus circulans. J. Mol. Cot. B: Enzymatic, in press.
    • J. Mol. Cot. B: Enzymatic
    • Kademi, A.1    Ait-Abdelkader, N.2    Fakhreddine, L.3    Baratti, J.4
  • 5
    • 0032904322 scopus 로고    scopus 로고
    • Molecular characterisation of the gene encoding an esterase from Bacillus licheniformis sharing significant similarities with lipases
    • Alvarez-Macarie, E., Augier-Magro, V., Guzzo, J., and Baratti, J., Molecular characterisation of the gene encoding an esterase from Bacillus licheniformis sharing significant similarities with lipases. Biotechnol Lett., 21, 313-319 (1999).
    • (1999) Biotechnol Lett. , vol.21 , pp. 313-319
    • Alvarez-Macarie, E.1    Augier-Magro, V.2    Guzzo, J.3    Baratti, J.4
  • 7
    • 0025914935 scopus 로고
    • Extracellular lipase of Pseudomonas sp. Strain ATCC 21808: Purification, characterization, crystallization, and preliminary X-ray diffraction data
    • Kordel, M., Hofmann, B., Schomburg, D., and Schmid, RD., Extracellular lipase of Pseudomonas sp. strain ATCC 21808: Purification, characterization, crystallization, and preliminary X-ray diffraction data. J. Bacteriol., 173, 4836-4841 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 4836-4841
    • Kordel, M.1    Hofmann, B.2    Schomburg, D.3    Schmid, R.D.4
  • 9
    • 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, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0028939811 scopus 로고
    • Purification and properties of three esterases from Brevibacterium sp. R312
    • Lambrechts, C., Escudero, J., and Galzy, P., Purification and properties of three esterases from Brevibacterium sp. R312. J. Appl. Bacteriol., 78:180-188 (1995).
    • (1995) J. Appl. Bacteriol. , vol.78 , pp. 180-188
    • Lambrechts, C.1    Escudero, J.2    Galzy, P.3
  • 12
    • 0026112861 scopus 로고
    • Isolation and partial characterisation of a novel thermostable carboxylesterase from a thermophilic
    • Owusu, R. K., and Cowan, D. A., Isolation and partial characterisation of a novel thermostable carboxylesterase from a thermophilic Bacillus. Enzym. Microb. Technol., 13, 158-163 (1991).
    • (1991) Bacillus. Enzym. Microb. Technol. , vol.13 , pp. 158-163
    • Owusu, R.K.1    Cowan, D.A.2
  • 14
    • 0025636149 scopus 로고
    • Production, purification and properties of extracellular carboxyl esterases from Bacillus subtilis NRRL 365
    • Meghji, K., Ward, O. P., and Araujo, A., Production, purification and properties of extracellular carboxyl esterases from Bacillus subtilis NRRL 365. Appl. Environ. Microbiol., 56, 3735-3740 (1990).
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3735-3740
    • Meghji, K.1    Ward, O.P.2    Araujo, A.3
  • 16
    • 0028281748 scopus 로고
    • Purification and characterisation of a thermostable carboxylesterase from the thermoacidophilic eubacterium
    • Manco, G., Di Gennaro, S., De Rosa, M., and Rossi, M., Purification and characterisation of a thermostable carboxylesterase from the thermoacidophilic eubacterium Bacillus acidocaldarius. Eur. J. Biochem., 221, 965-972 (1994).
    • (1994) Bacillus Acidocaldarius. Eur. J. Biochem. , vol.221 , pp. 965-972
    • Manco, G.1    Di Gennaro, S.2    De Rosa, M.3    Rossi, M.4
  • 17
    • 0023971213 scopus 로고
    • Purification and characterisation of a heat-stable esterase from the thermoacidophilic archaebacteri-um
    • Sobek, H., and Gorisch, H., Purification and characterisation of a heat-stable esterase from the thermoacidophilic archaebacteri-um Sulfolobus acidocaldarius. Biochem. J., 250, 453-458 (1988).
    • (1988) Sulfolobus Acidocaldarius. Biochem. J. , vol.250 , pp. 453-458
    • Sobek, H.1    Gorisch, H.2
  • 18
    • 0024710697 scopus 로고
    • Further kinetic and molecular characterisation of an extremely heat-stable carboxylesterase from the thermoacidophilic archaebacterium
    • Sobek, H., and Gorisch, H., Further kinetic and molecular characterisation of an extremely heat-stable carboxylesterase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biochem. J., 261, 993-998 (1989).
    • (1989) Sulfolobus Acidocaldarius. Biochem. J. , vol.261 , pp. 993-998
    • Sobek, H.1    Gorisch, H.2
  • 20
    • 0026549769 scopus 로고
    • In vivo processing of Staphylococcus aureus lipase
    • Rollof, J., and Normark, S., In vivo processing of Staphylococcus aureus lipase. J. Bacteriol., 174, 1844-1847 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 1844-1847
    • Rollof, J.1    Normark, S.2
  • 22
    • 0027325860 scopus 로고
    • The classification of hydrolases that hydrolyse or-ganophosphates: Recent developments
    • Walker, C. H., The classification of hydrolases that hydrolyse or-ganophosphates: Recent developments. Chem. Biol. Interne., 87, 17-24 (1993).
    • (1993) Chem. Biol. Interne. , vol.87 , pp. 17-24
    • Walker, C.H.1
  • 24
    • 0026638399 scopus 로고
    • Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168
    • Dartois, V., Baulard, A., Schanck, K., and Colson, C., Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168. Biochim. Biophys. Acta, 1131, 253-260 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 253-260
    • Dartois, V.1    Baulard, A.2    Schanck, K.3    Colson, C.4
  • 27
    • 0026033986 scopus 로고
    • Purification and characterisation of mono- and diacylglycerol lipase isolated from Penicillium camembertii U-150
    • Yamaguchi, S., and Mase, T., Purification and characterisation of mono- and diacylglycerol lipase isolated from Penicillium camembertii U-150. Appl. Microbiol. Biotechnol., 34, 720-725 (1991).
    • (1991) Appl. Microbiol. Biotechnol. , vol.34 , pp. 720-725
    • Yamaguchi, S.1    Mase, T.2
  • 28
    • 0001337212 scopus 로고
    • Purification and some characteristics of extracellular lipase from Fusarium oxysporum f. sp. Lini. Biosci
    • Hoshino, T., Sasaki, T., Watanabe, Y., Nagasawa, T., and Yamane, T., Purification and some characteristics of extracellular lipase from Fusarium oxysporum f. sp. lini. Biosci. Biotechnol. Biochem., 56, 660-664 (1992).
    • (1992) Lini. Biosci. Biotechnol. Biochem. , vol.56 , pp. 660-664
    • Hoshino, T.1    Sasaki, T.2    Watanabe, Y.3    Nagasawa, T.4    Yamane, T.5
  • 30
    • 0027200087 scopus 로고
    • Interfacial activation of the li-pase-procolipase complex by mixed micelles revealed by X-ray crystallography
    • van Tilbeurgh, H., Egloff, M. P., Martinez, C., Rugani, N., Verger, R., and Cambillau, C., Interfacial activation of the li-pase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature, 362, 814-820 (1993).
    • (1993) Nature , vol.362 , pp. 814-820
    • Van Tilbeurgh, H.1    Egloff, M.P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 31
    • 0028922084 scopus 로고
    • A bacterial esterase is homologous with non-haem haloperoxidases and displays brominating activity
    • Pelletier, I., and Altenbuchner, J., A bacterial esterase is homologous with non-haem haloperoxidases and displays brominating activity. Microbiology, 141, 459-468 (1995).
    • (1995) Microbiology , vol.141 , pp. 459-468
    • Pelletier, I.1    Altenbuchner, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.