메뉴 건너뛰기




Volumn 22, Issue 2, 1998, Pages 86-93

Enantioselectivity of Pseudomonas cepacia and Candida rugosa lipases for the resolution of secondary alcohols: The effect of Candida rugosa isoenzymes

Author keywords

Alcoholysis; Candida rugosa; Enantioselectivity; Hydrolysis; Isoenzymes; Lipase; Pseudomonas cepacia; Resolution

Indexed keywords

ALCOHOLS; BACTERIA; BIOTECHNOLOGY; CATALYSIS; ENZYMES; ESTERS; FRACTIONATION; FUNGI; HYDROLYSIS;

EID: 0032007895     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(97)00104-X     Document Type: Article
Times cited : (48)

References (30)
  • 1
    • 33751499686 scopus 로고
    • A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from pseudomonas cepacia and lipase from Candida rugosa
    • 1. Kazlauskas, R. J., Weissfloch, A. N. E., Rappaport, A. T., and Cuccia, L. A. A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia and lipase from Candida rugosa. J. Org. Chem. 1991, 56, 2656-2665
    • (1991) J. Org. Chem. , vol.56 , pp. 2656-2665
    • Kazlauskas, R.J.1    Weissfloch, A.N.E.2    Rappaport, A.T.3    Cuccia, L.A.4
  • 2
    • 33751390847 scopus 로고
    • Lipase-catalyzed enantioselective transesterification of O-trityl 1, 2-diols. Practical synthesis of (R)-tritylglycidol
    • 2. Kim, M.-J. and Choi, Y. K. Lipase-catalyzed enantioselective transesterification of O-trityl 1, 2-diols. Practical synthesis of (R)-tritylglycidol. J. Org. Chem. 1992, 57, 1605-1607
    • (1992) J. Org. Chem. , vol.57 , pp. 1605-1607
    • Kim, M.-J.1    Choi, Y.K.2
  • 4
    • 0000486075 scopus 로고
    • Alcohol induced reversal of enantioselectivity in a lipase catalyzed resolution of 2-chloropropionic acid
    • 4. Holmberg, E. and Hult, K. Alcohol induced reversal of enantioselectivity in a lipase catalyzed resolution of 2-chloropropionic acid. Biocatalysis 1992, 5, 289-296
    • (1992) Biocatalysis , vol.5 , pp. 289-296
    • Holmberg, E.1    Hult, K.2
  • 5
    • 0001484267 scopus 로고
    • Enantioselectivity of Candida rugosa lipase toward carboxylic acids: A predictive rule from substrate mapping and X-ray crystallography
    • 5. Ahmed, S. N., Kazlauskas, R. J., Morinville, A. H., Grochulski, P., Schrag, J. D., and Cygler, M. Enantioselectivity of Candida rugosa lipase toward carboxylic acids: A predictive rule from substrate mapping and X-ray crystallography. Biocatalysis 1994, 9, 209-225
    • (1994) Biocatalysis , vol.9 , pp. 209-225
    • Ahmed, S.N.1    Kazlauskas, R.J.2    Morinville, A.H.3    Grochulski, P.4    Schrag, J.D.5    Cygler, M.6
  • 6
    • 33751155794 scopus 로고
    • A 2-propanol treatment increases the enantioselectivity of Candida rugosa lipase toward esters of chiral carboxylic acids
    • 6. Colton, I. J., Ahmed, S. N., and 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
  • 7
    • 0030019835 scopus 로고    scopus 로고
    • Resolution of a tetrahydrofuran ester by Candida rugosa lipase (CRL) and an examination of CRL's stereochemical preference in organic media
    • 7. Franssen, M. C. R., Jongejan, H., Kooijman, H., Spek, A. L., Mondril, N. L. F. L. C., dos Santos, P. M. A. C. B., and de Groot, A. Resolution of a tetrahydrofuran ester by Candida rugosa lipase (CRL) and an examination of CRL's stereochemical preference in organic media. Tetrahedron Asym. 1996, 7, 497-510
    • (1996) Tetrahedron Asym. , vol.7 , pp. 497-510
    • Franssen, M.C.R.1    Jongejan, H.2    Kooijman, H.3    Spek, A.L.4    Mondril, N.L.F.L.C.5    Dos Santos, P.M.A.C.B.6    De Groot, A.7
  • 8
    • 37049087281 scopus 로고
    • Lipase catalysis in the optical resolution of 2-amino-1-phenylethanol derivatives
    • 8. Kanerva, L. T., Rahiala, K., and Vänttinen, E. Lipase catalysis in the optical resolution of 2-amino-1-phenylethanol derivatives. J. Chem. Soc. Perkin 1 1992, 1759-1762
    • (1992) J. Chem. Soc. Perkin 1 , pp. 1759-1762
    • Kanerva, L.T.1    Rahiala, K.2    Vänttinen, E.3
  • 9
    • 0029143582 scopus 로고
    • Enantiomers of ring-substituted 2-amino-1-phenylethanols by pseudomonas cepacia lipase
    • 9. Lundell, K. and Kanerva, L. T. Enantiomers of ring-substituted 2-amino-1-phenylethanols by Pseudomonas cepacia lipase. Tetrahedron Asym. 1995, 6, 2281-2286
    • (1995) Tetrahedron Asym. , vol.6 , pp. 2281-2286
    • Lundell, K.1    Kanerva, L.T.2
  • 10
    • 0000384421 scopus 로고
    • Optically active cyanohydrins and enzyme catalysis
    • 10. Kanerva, L. T., Rahiala, K., and Sundholm, O. Optically active cyanohydrins and enzyme catalysis. Biocatalysis 1994, 10, 169-180
    • (1994) Biocatalysis , vol.10 , pp. 169-180
    • Kanerva, L.T.1    Rahiala, K.2    Sundholm, O.3
  • 11
    • 0027451329 scopus 로고
    • Enzymatic resolution of optically active aliphatic cyanohydrins
    • 11. Kanerva, L. T., Kiljunen, E., and Huuhtanen, T. Enzymatic resolution of optically active aliphatic cyanohydrins. Tetrahedron Asym. 1993, 4, 2355-2361
    • (1993) Tetrahedron Asym. , vol.4 , pp. 2355-2361
    • Kanerva, L.T.1    Kiljunen, E.2    Huuhtanen, T.3
  • 12
    • 0001262017 scopus 로고
    • Resolution of secondary alcohols using lipase in diisopropyl ether
    • 12. Bevinakatti, H. S., Banerji, A. A., and Newadkar, R. V. Resolution of secondary alcohols using lipase in diisopropyl ether. J. Org. Chem. 1989, 54, 2453-2455
    • (1989) J. Org. Chem. , vol.54 , pp. 2453-2455
    • Bevinakatti, H.S.1    Banerji, A.A.2    Newadkar, R.V.3
  • 13
    • 0022966109 scopus 로고
    • Asymmetric hydrolysis of (dl)-1-acyloxy-2-halo-1-phenylethanes with lipases
    • 13. Kutsuki, H., Sawa, I., Hasegawa, J., and Watanabe, K. Asymmetric hydrolysis of (dl)-1-Acyloxy-2-halo-1-phenylethanes with lipases. Agric. Biol. Chem. 1986, 50, 2369-2373
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 2369-2373
    • Kutsuki, H.1    Sawa, I.2    Hasegawa, J.3    Watanabe, K.4
  • 15
    • 0017390556 scopus 로고
    • A rapid, sensitive and versatile assay for protein using coomassie brilliant blue G-250
    • 15. Sedmak, J. J. and Grossberg, S. E. A rapid, sensitive and versatile assay for protein using Coomassie Brilliant Blue G-250. Anal. Biochem. 1977, 79, 544-552
    • (1977) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 16
    • 37049079149 scopus 로고
    • Enzymatic acylation in the resolution of methyl threo-2-hydroxy-3-(4-methoxyphenyl)-3-(2-X-phenylthio)propionates in organic solvents
    • 16. Kanerva, L. T. and Sundholm, O. Enzymatic acylation in the resolution of methyl threo-2-hydroxy-3-(4-methoxyphenyl)-3-(2-X-phenylthio)propionates in organic solvents. J. Chem. Soc. Perkin 1 1993, 2407-2410
    • (1993) J. Chem. Soc. Perkin 1 , pp. 2407-2410
    • Kanerva, L.T.1    Sundholm, O.2
  • 17
    • 0024805184 scopus 로고
    • Characterization of three distinct forms of lipolytic activity in a commercial Candida lipase preparation
    • 17. Shaw, J. J., Chang, C. H., and Wang, Y. J. Characterization of three distinct forms of lipolytic activity in a commercial Candida lipase preparation. Biotechnol. Lett. 1989, 11, 779-784
    • (1989) Biotechnol. Lett. , vol.11 , pp. 779-784
    • Shaw, J.J.1    Chang, C.H.2    Wang, Y.J.3
  • 18
    • 34249967848 scopus 로고
    • Detection and partial purification of two lipases from Candida rugosa
    • 18. Veeraragavan, K. and Gibbs, B. F. Detection and partial purification of two lipases from Candida rugosa. Biotechnol. Lett. 1989, 11, 345-348
    • (1989) Biotechnol. Lett. , vol.11 , pp. 345-348
    • Veeraragavan, K.1    Gibbs, B.F.2
  • 20
    • 0024489264 scopus 로고
    • Effects on chemical modification of amino acid residues on the activities of lipase from Candida cylindracea
    • 20. Kawase, M. and Tanaka, A. Effects on chemical modification of amino acid residues on the activities of lipase from Candida cylindracea. Enzyme Microb. Technol. 1989, 11, 44-48
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 44-48
    • Kawase, M.1    Tanaka, A.2
  • 21
    • 0025284519 scopus 로고
    • Enhancing the enantioselectivity of Candida lipase-catalyzed ester hydrolysis via noncovalent enzyme modification
    • 21. Wu, S.-H., Guo, Z.-W., and Sih, C. J. Enhancing the enantioselectivity of Candida lipase-catalyzed ester hydrolysis via noncovalent enzyme modification. J. Am. Chem. Soc. 1990, 112, 1990-1995
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1990-1995
    • Wu, S.-H.1    Guo, Z.-W.2    Sih, C.J.3
  • 22
    • 0014310082 scopus 로고
    • Size and charge isomer separation and estimation of molecular weight of proteins by disc gel electrophoresis
    • 22. Hedrick, J. L. and Smith, A. J. Size and charge isomer separation and estimation of molecular weight of proteins by disc gel electrophoresis. Arch. Biochem. Biophys. 1968, 126, 155-164
    • (1968) Arch. Biochem. Biophys. , vol.126 , pp. 155-164
    • Hedrick, J.L.1    Smith, A.J.2
  • 23
    • 0010429165 scopus 로고
    • Studies on lipase from Candida cylindracea part I. Purification and properties
    • 23. Tomizuka, N., Ota, Y., and Yamada, K. Studies on lipase from Candida cylindracea Part I. Purification and properties. Agric. Biol. Chem. 1966, 30, 576-584
    • (1966) Agric. Biol. Chem. , vol.30 , pp. 576-584
    • Tomizuka, N.1    Ota, Y.2    Yamada, K.3
  • 24
    • 0000109370 scopus 로고
    • Studies of the heterogeneity of a Candida cylindracea (rugosa) lipase: Monitoring of esterolytic activity and enantioselectivity by chiral liquid chromatography
    • 24. Allenmark, S. and Ohlsson, A. Studies of the heterogeneity of a Candida cylindracea (rugosa) lipase: Monitoring of esterolytic activity and enantioselectivity by chiral liquid chromatography. Biocatalysis 1992, 6, 211-221
    • (1992) Biocatalysis , vol.6 , pp. 211-221
    • Allenmark, S.1    Ohlsson, A.2
  • 25
    • 20644469267 scopus 로고
    • Quantitative analyses of biochemical kinetic resolutions of enantiomers
    • 25. Chen, C. S., Fujimoto, Y., Girdaukas, G., and Sih, C. J. Quantitative analyses of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc. 1982, 104, 7294-7299
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7294-7299
    • Chen, C.S.1    Fujimoto, Y.2    Girdaukas, G.3    Sih, C.J.4
  • 26
    • 0003045944 scopus 로고    scopus 로고
    • Hydrolase-catalysed asymmetric and other transformations of synthetic interest
    • (Koskinen, A. M. P. and Klibanov, A. M., Eds.). Chapman & Hall, London
    • 26. Kanerva, L. T. Hydrolase-catalysed asymmetric and other transformations of synthetic interest. In: Enzymatic Reactions in Organic Media (Koskinen, A. M. P. and Klibanov, A. M., Eds.). Chapman & Hall, London, 1996, 170-223
    • (1996) Enzymatic Reactions in Organic Media , pp. 170-223
    • Kanerva, L.T.1
  • 27
    • 0000218831 scopus 로고
    • Enzymatic preparation of optically active α-and β-hydroxy carboxylic acid derivatives
    • 27. Kanerva, L. T. and Sundholm, O. Enzymatic preparation of optically active α-and β-hydroxy carboxylic acid derivatives. Acta Chem. Scand. 1993, 47, 823-825
    • (1993) Acta Chem. Scand. , vol.47 , pp. 823-825
    • Kanerva, L.T.1    Sundholm, O.2
  • 28
    • 0028015905 scopus 로고
    • Comparison of the enzymatic activity of commercial and semipurified lipase of Candida cylindracea in the hydrolysis of the esters of (R,S) 2-aryl propionic acids
    • 28. Hernáiz, M. J., Sánchez-Montero, J. M., and Sinisterra, J. V. Comparison of the enzymatic activity of commercial and semipurified lipase of Candida cylindracea in the hydrolysis of the esters of (R,S) 2-aryl propionic acids. Tetrahedron 1994, 50, 10749-10760
    • (1994) Tetrahedron , vol.50 , pp. 10749-10760
    • Hernáiz, M.J.1    Sánchez-Montero, J.M.2    Sinisterra, J.V.3
  • 29
    • 0029141885 scopus 로고
    • Hydrolysis of (R,S)-2-aryl propionic esters by pure lipase B from Candida cylindracea
    • 29. Hernáiz, M. J., Sánchez-Montero, J. M., and Sinisterra, J. V. Hydrolysis of (R,S)-2-aryl propionic esters by pure lipase B from Candida cylindracea. J. Mol. Catalysis A: Chem. 1995, 96, 317-327
    • (1995) J. Mol. Catalysis A: Chem. , vol.96 , pp. 317-327
    • Hernáiz, M.J.1    Sánchez-Montero, J.M.2    Sinisterra, J.V.3
  • 30
    • 0028075638 scopus 로고
    • Elucidating structure-mechanism relationships in lipases: Prospects for predicting and engineering catalytic properties
    • 30. Kazlauskas, R. J. Elucidating structure-mechanism relationships in lipases: Prospects for predicting and engineering catalytic properties. TIBTECH 1994, 12, 464-472
    • (1994) TIBTECH , vol.12 , pp. 464-472
    • Kazlauskas, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.