메뉴 건너뛰기




Volumn 19, Issue 3, 1996, Pages 181-186

Lipase-catalyzed kinetic resolution of 3-hydroxy esters in organic solvents and supercritical carbon dioxide

Author keywords

3 hydroxy esters; Kinetic resolution; Lipase; Organic solvents; Pseudomonas cepacia; Supercritical carbon dioxide

Indexed keywords

CARBON DIOXIDE; ENZYME IMMOBILIZATION; ENZYMES; ESTERIFICATION; ESTERS; MOLECULAR SIEVES; ORGANIC SOLVENTS; STABILITY; SUPERCRITICAL FLUID EXTRACTION;

EID: 0030586805     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/0141-0229(95)00229-4     Document Type: Article
Times cited : (35)

References (14)
  • 2
    • 0027112083 scopus 로고
    • Kinetics of lipase-catalyzed esterification in supercritical carbon dioxide
    • 2. Marty, A., Chulalaksananukul, W., Willemot, R. M., and Condorét, S. Kinetics of lipase-catalyzed esterification in supercritical carbon dioxide. Biotechnol. Bioeng. 1992, 39, 273-280
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 273-280
    • Marty, A.1    Chulalaksananukul, W.2    Willemot, R.M.3    Condorét, S.4
  • 4
    • 0001384739 scopus 로고
    • Lipase catalyzed esterification of glycidol in chloroform and in supercritical carbon dioxide
    • 4. Martins, J. F., Sampaio, T. C., Carvalho, I. B., da Ponte, M. N., and Barreiros, S. Lipase catalyzed esterification of glycidol in chloroform and in supercritical carbon dioxide. High Press. Biotechnol. 1992, 224, 411-415
    • (1992) High Press. Biotechnol. , vol.224 , pp. 411-415
    • Martins, J.F.1    Sampaio, T.C.2    Carvalho, I.B.3    Da Ponte, M.N.4    Barreiros, S.5
  • 6
    • 0028420065 scopus 로고
    • Enantioselectivity and reactivity of immobilized lipase in supercritical carbon dioxide
    • 6. Cernia, E., Palocci, C., Gasparrini, F., Misiti, D., and Fagnano, N. Enantioselectivity and reactivity of immobilized lipase in supercritical carbon dioxide. J. Mol. Catal. 1994, 89, L11-L18
    • (1994) J. Mol. Catal. , vol.89
    • Cernia, E.1    Palocci, C.2    Gasparrini, F.3    Misiti, D.4    Fagnano, N.5
  • 8
    • 84985689397 scopus 로고
    • Use of the zinc-copper couple in the Reformatskii reaction
    • 8. Santaniello, E. and Manzocchi, A. Use of the zinc-copper couple in the Reformatskii reaction. Synthesis 1977, 10, 698-699
    • (1977) Synthesis , vol.10 , pp. 698-699
    • Santaniello, E.1    Manzocchi, A.2
  • 9
    • 33845282987 scopus 로고
    • Quantitative analyses of biochemical kinetic resolution of enantiomers. 2. Enzyme-catalyzed esterifications in water-organic solvent biphasic systems
    • 9. Chen, C. S., Wu, S. H., Girdaukas, G., and Sih, C. J. Quantitative analyses of biochemical kinetic resolution of enantiomers. 2. Enzyme-catalyzed esterifications in water-organic solvent biphasic systems. J. Am. Chem. Soc. 1987, 109, 2812-2817
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2812-2817
    • Chen, C.S.1    Wu, S.H.2    Girdaukas, G.3    Sih, C.J.4
  • 10
    • 0029160746 scopus 로고
    • Sensitivity of microbial lipases to acetaldehyde formed by acyl-transfer reactions from vinyl esters
    • 10. Weber, H. K., Stecher, H., and Faber, K. Sensitivity of microbial lipases to acetaldehyde formed by acyl-transfer reactions from vinyl esters. Biotechnol. Lett. 1995, 17, 803-808
    • (1995) Biotechnol. Lett. , vol.17 , pp. 803-808
    • Weber, H.K.1    Stecher, H.2    Faber, K.3
  • 11
    • 85004271190 scopus 로고
    • Enzymatic interesterification in supercritical carbon dioxide
    • 11. Chi, Y. M, Nakamura, K., and Yano, T. Enzymatic interesterification in supercritical carbon dioxide. Agric. Biol. Chem. 1988, 52, 1541-1550
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1541-1550
    • Chi, Y.M.1    Nakamura, K.2    Yano, T.3
  • 12
    • 0027112426 scopus 로고
    • Biocatalytic synthesis of acrylates in organic solvents and supercritical fluids. I. Optimization of enzyme environment
    • 12. Kamat, S., Barrera, J., Beckman, E. J., and Russell, A. J. Biocatalytic synthesis of acrylates in organic solvents and supercritical fluids. I. Optimization of enzyme environment. Biotechnol. Bioeng. 1992, 40, 158-166
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 158-166
    • Kamat, S.1    Barrera, J.2    Beckman, E.J.3    Russell, A.J.4
  • 13
    • 0026881145 scopus 로고
    • Enzymatic reaction kinetic: Comparison in an organic solvent and supercritical carbon dioxide
    • 13. Dumont, T., Barth, D., Corbier, C., Branlant, G., and Perrut, M. Enzymatic reaction kinetic: Comparison in an organic solvent and supercritical carbon dioxide. Biotechnol. Bioeng. 1992, 39, 329-333
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 329-333
    • Dumont, T.1    Barth, D.2    Corbier, C.3    Branlant, G.4    Perrut, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.