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Volumn 64, Issue , 2012, Pages 55-60

Purification and characterization of an organic solvent-stable lipase from Pseudomonas stutzeri LC2-8 and its application for efficient resolution of (R, S)-1-phenylethanol

Author keywords

Biocatalysis; Enantioseparation; Lipase; Organic solvent stability; Pseudomonas stutzeri; Purification

Indexed keywords

AMINO ACID RESIDUES; ANION EXCHANGE CHROMATOGRAPHY; BIOCATALYSIS; ENANTIOMERIC EXCESS; ENANTIOSEPARATIONS; HYDROLYTIC ACTIVITIES; HYDROPHILIC SOLVENTS; ISO-PROPANOLS; LIPASE ACTIVITY; NON-AQUEOUS SYSTEM; OPEN READING FRAME; OPTIMUM PH; ORGANIC SOLVENT-STABILITY; PHENYLETHANOL; PSEUDOMONAS STUTZERI; SDS-PAGE;

EID: 84859846840     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2012.03.004     Document Type: Article
Times cited : (53)

References (19)
  • 1
    • 0346958289 scopus 로고    scopus 로고
    • Organic solvent tolerant lipase by Pseudomonas sp strain S5: stability of enzyme in organic solvent and physical factors affecting its production
    • Baharum S.N., Salleh A.B., Razak C.N.A., Basri M., Rahman M.B.A., Rahman R. Organic solvent tolerant lipase by Pseudomonas sp strain S5: stability of enzyme in organic solvent and physical factors affecting its production. Ann. Microbiol. 2003, 53:75-83.
    • (2003) Ann. Microbiol. , vol.53 , pp. 75-83
    • Baharum, S.N.1    Salleh, A.B.2    Razak, C.N.A.3    Basri, M.4    Rahman, M.B.A.5    Rahman, R.6
  • 2
    • 0022724718 scopus 로고
    • Enzymes that work in organic solvents
    • Klibanov A.M. Enzymes that work in organic solvents. Chem. Tech. 1986, 16:354-359.
    • (1986) Chem. Tech. , vol.16 , pp. 354-359
    • Klibanov, A.M.1
  • 3
    • 0028018145 scopus 로고
    • Organic-solvent-tolerant bacterium which secretes organic-solvent-stable lipolytic enzyme
    • Ogino H., Miyamoto K., Ishikawa H. Organic-solvent-tolerant bacterium which secretes organic-solvent-stable lipolytic enzyme. Appl. Environ. Microbiol. 1994, 60:3884-3886.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3884-3886
    • Ogino, H.1    Miyamoto, K.2    Ishikawa, H.3
  • 4
    • 0038745326 scopus 로고    scopus 로고
    • A newly isolated organic solvent tolerant Bacillus sphaericus 205y producing organic solvent-stable lipase
    • Hun C.J., Rahman R., Salleh A.B., Basri M. A newly isolated organic solvent tolerant Bacillus sphaericus 205y producing organic solvent-stable lipase. Biochem. Eng. J. 2003, 15:147-151.
    • (2003) Biochem. Eng. J. , vol.15 , pp. 147-151
    • Hun, C.J.1    Rahman, R.2    Salleh, A.B.3    Basri, M.4
  • 5
    • 42749092984 scopus 로고    scopus 로고
    • Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010
    • Zhao L.L., Xu J.H., Zhao J., Pan J., Wang Z.L. Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010. Process Biochem. 2008, 43:626-633.
    • (2008) Process Biochem. , vol.43 , pp. 626-633
    • Zhao, L.L.1    Xu, J.H.2    Zhao, J.3    Pan, J.4    Wang, Z.L.5
  • 6
    • 0018399632 scopus 로고
    • Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by serratia-marcescens
    • Winkler U.K., Stuckmann M. Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by serratia-marcescens. J. Bacteriol. 1979, 138:663-670.
    • (1979) J. Bacteriol. , vol.138 , pp. 663-670
    • Winkler, U.K.1    Stuckmann, M.2
  • 7
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 9
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J.C., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 11
    • 0033917914 scopus 로고    scopus 로고
    • Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03
    • Ogino H., Nakagawa S., Shinya K., Muto T., Fujimura N., Yasuda M., Ishikawa H. Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03. J. Biosci. Bioeng. 2000, 89:451-457.
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 451-457
    • Ogino, H.1    Nakagawa, S.2    Shinya, K.3    Muto, T.4    Fujimura, N.5    Yasuda, M.6    Ishikawa, H.7
  • 12
    • 75349100918 scopus 로고    scopus 로고
    • Organic solvent-tolerant enzymes
    • Doukyu N., Ogino H. Organic solvent-tolerant enzymes. Biochem. Eng. J. 2010, 48:270-282.
    • (2010) Biochem. Eng. J. , vol.48 , pp. 270-282
    • Doukyu, N.1    Ogino, H.2
  • 13
    • 0035108407 scopus 로고    scopus 로고
    • Enzymes which are stable in the presence of organic solvents
    • Ogino H., Ishikawa H. Enzymes which are stable in the presence of organic solvents. J. Biosci. Bioeng. 2001, 91:109-116.
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 109-116
    • Ogino, H.1    Ishikawa, H.2
  • 14
    • 57449118547 scopus 로고    scopus 로고
    • Cloning, expression and characterization of an organic solvent tolerant lipase from Pseudomonas fluorescens JCM5963
    • Zhang A.J., Gao R.J., Diao N.B., Xie G.Q., Gao G., Cao S.G. Cloning, expression and characterization of an organic solvent tolerant lipase from Pseudomonas fluorescens JCM5963. J. Mol. Catal. B: Enzym. 2009, 56:78-84.
    • (2009) J. Mol. Catal. B: Enzym. , vol.56 , pp. 78-84
    • Zhang, A.J.1    Gao, R.J.2    Diao, N.B.3    Xie, G.Q.4    Gao, G.5    Cao, S.G.6
  • 15
    • 67649283612 scopus 로고    scopus 로고
    • Homologous expression, purification and characterization of a novel high-alkaline and thermal stable lipase from Burkholderia cepacia ATCC 25416
    • Wang X.Q., Yu X.W., Xu Y. Homologous expression, purification and characterization of a novel high-alkaline and thermal stable lipase from Burkholderia cepacia ATCC 25416. Enzyme Microb. Technol. 2009, 45:94-102.
    • (2009) Enzyme Microb. Technol. , vol.45 , pp. 94-102
    • Wang, X.Q.1    Yu, X.W.2    Xu, Y.3
  • 16
    • 33751155794 scopus 로고
    • A 2-propanol treatment increases the enantioselectivity of Candida rugosa lipase toward esters of chiral carboxylic acids
    • Colton I.J., Ahmed S.N., Kazlauskas R.J. A 2-propanol treatment increases the enantioselectivity of Candida rugosa lipase toward esters of chiral carboxylic acids. J. Org. Chem. 1995, 60:212-217.
    • (1995) J. Org. Chem. , vol.60 , pp. 212-217
    • Colton, I.J.1    Ahmed, S.N.2    Kazlauskas, R.J.3
  • 17
    • 34447104110 scopus 로고    scopus 로고
    • Overexpression of Serratia marcescens lipase in Escherichia coli for efficient bioresolution of racemic ketoprofen
    • Long Z.D., Xu J.H., Zhao L.L., Pan J., Yang S., Hua L. Overexpression of Serratia marcescens lipase in Escherichia coli for efficient bioresolution of racemic ketoprofen. J. Mol. Catal. B: Enzym. 2007, 47:105-110.
    • (2007) J. Mol. Catal. B: Enzym. , vol.47 , pp. 105-110
    • Long, Z.D.1    Xu, J.H.2    Zhao, L.L.3    Pan, J.4    Yang, S.5    Hua, L.6
  • 18
    • 63249106284 scopus 로고    scopus 로고
    • Optimization of (R, S)-l-phenylethanol kinetic resolution over Candida antarctica lipase B in ionic liquids
    • Habulin, Maja, Knez, Zeljko Optimization of (R, S)-l-phenylethanol kinetic resolution over Candida antarctica lipase B in ionic liquids. J. Mol. Catal. B: Enzym. 2009, 58:24-28.
    • (2009) J. Mol. Catal. B: Enzym. , vol.58 , pp. 24-28
    • Habulin1    Maja2    Knez3    Zeljko4
  • 19
    • 34447650583 scopus 로고    scopus 로고
    • Lipase immobilized on HOOC-MCF: a highly enantioselective catalyst for transesterification resolution of (R, S)-1-phenylethanol
    • Xue P., Yan X.H., Wang Z. Lipase immobilized on HOOC-MCF: a highly enantioselective catalyst for transesterification resolution of (R, S)-1-phenylethanol. Chin. Chem. Lett. 2007, 18:929-932.
    • (2007) Chin. Chem. Lett. , vol.18 , pp. 929-932
    • Xue, P.1    Yan, X.H.2    Wang, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.