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Volumn 55, Issue 11, 2000, Pages 2001-2008

Modelling of two enzyme reactions in a linked cofactor recycle system for chiral lactone synthesis

Author keywords

Biocatalysis; Cyclohexanone monooxygenase; Enzyme; Mathematical modelling; NADPH; Reaction engineering

Indexed keywords

BIOSYNTHESIS; CATALYSIS; KETONES; MATHEMATICAL MODELS; NUMERICAL METHODS; OPTIMIZATION; PH EFFECTS; RATE CONSTANTS;

EID: 0034108772     PISSN: 00092509     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2509(99)00478-9     Document Type: Article
Times cited : (35)

References (24)
  • 4
    • 0027625031 scopus 로고
    • Kinetic models for synthesis by a thermophilic alcohol dehydrogenase
    • Ford J.B., Askins K.J., Taylor K.B. Kinetic models for synthesis by a thermophilic alcohol dehydrogenase. Biotechnology and Bioengineering. 42:1993;367-375.
    • (1993) Biotechnology and Bioengineering , vol.42 , pp. 367-375
    • Ford, J.B.1    Askins, K.J.2    Taylor, K.B.3
  • 5
    • 0343838273 scopus 로고    scopus 로고
    • Biocatalytic Baeyer-Villiger characterisation leading to reactor design
    • IChemE, Rugby, UK
    • Hogan, M.C., Woodley, J.M., & Lilly, M.D. (1998). Biocatalytic Baeyer-Villiger characterisation leading to reactor design. Proceedings of the 1998 IChemE Research Event, IChemE, Rugby, UK, pp. 466-514.
    • (1998) Proceedings of the 1998 IChemE Research Event , pp. 466-514
    • Hogan, M.C.1    Woodley, J.M.2    Lilly, M.D.3
  • 6
    • 0025438142 scopus 로고
    • Sorbitol production in charged membrane bioreactor with coenzyme regeneration system: 2. Theoretical analysis of a continuous reaction with retained and regenerated NADPH
    • Ikemi M., Koizumi N., Ishimatsu Y. Sorbitol production in charged membrane bioreactor with coenzyme regeneration system. 2. Theoretical analysis of a continuous reaction with retained and regenerated NADPH Biotechnology and Bioengineering. 36:1990;155-165.
    • (1990) Biotechnology and Bioengineering , vol.36 , pp. 155-165
    • Ikemi, M.1    Koizumi, N.2    Ishimatsu, Y.3
  • 7
    • 0001230359 scopus 로고
    • Thermostable enzymes in organic synthesis. Asymmetric reduction of ketones with alcohol dehydrogenase from Thermoanaerobium brockii
    • Keinan E., Hafeli E.K., Seth K.K., Lamed R. Thermostable enzymes in organic synthesis. Asymmetric reduction of ketones with alcohol dehydrogenase from Thermoanaerobium brockii. Journal of the American Chemical Society. 108:1986;162-169.
    • (1986) Journal of the American Chemical Society , vol.108 , pp. 162-169
    • Keinan, E.1    Hafeli, E.K.2    Seth, K.K.3    Lamed, R.4
  • 8
    • 0029891893 scopus 로고    scopus 로고
    • Continuous production of L-tert-leucine in series of two enzyme membrane reactors, modelling and computer simulation
    • Kragl U., Vasic-Racki D., Wandrey C. Continuous production of L-tert-leucine in series of two enzyme membrane reactors, modelling and computer simulation. Bioprocess Engineering. 14:1996;291-297.
    • (1996) Bioprocess Engineering , vol.14 , pp. 291-297
    • Kragl, U.1    Vasic-Racki, D.2    Wandrey, C.3
  • 9
    • 0019554401 scopus 로고
    • Novel NADP linked alcohol-aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria
    • Lamed R.J., Zeikus J.G. Novel NADP linked alcohol-aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria. Biochemical Journal. 195:1981;183-190.
    • (1981) Biochemical Journal , vol.195 , pp. 183-190
    • Lamed, R.J.1    Zeikus, J.G.2
  • 12
    • 0006735358 scopus 로고    scopus 로고
    • Biotransformations for fine chemical production
    • Meyer H.P., Kiener A., Imwinkelried R., Shaw N. Biotransformations for fine chemical production. Chimia. 51:1997;287-289.
    • (1997) Chimia , vol.51 , pp. 287-289
    • Meyer, H.P.1    Kiener, A.2    Imwinkelried, R.3    Shaw, N.4
  • 13
    • 0343494910 scopus 로고    scopus 로고
    • Steady state kinetic mechanism of Thermoanaerobium brockii alcohol dehydrogenase: A study of discrimination between alternative kinetic models
    • Oestreicher E.O., Pereira D.A., Pinto G.F. Steady state kinetic mechanism of Thermoanaerobium brockii alcohol dehydrogenase. a study of discrimination between alternative kinetic models Journal of Biotechnology. 46:1996;23-31.
    • (1996) Journal of Biotechnology , vol.46 , pp. 23-31
    • Oestreicher, E.O.1    Pereira, D.A.2    Pinto, G.F.3
  • 14
    • 0028222913 scopus 로고
    • Kinetic mechanism of the oxidation of 2-propanol catalysed by Thermoanaerobium brockii alcohol dehydrogenase
    • Pereira D.A., Pinto G.F., Oestreicher E.O. Kinetic mechanism of the oxidation of 2-propanol catalysed by Thermoanaerobium brockii alcohol dehydrogenase. Journal of Biotechnology. 34:1994;43-50.
    • (1994) Journal of Biotechnology , vol.34 , pp. 43-50
    • Pereira, D.A.1    Pinto, G.F.2    Oestreicher, E.O.3
  • 15
    • 0020490705 scopus 로고
    • Mechanistic studies on cyclohexanone monooxygenase
    • Ryerson C.C., Ballou D.P., Walsh C. Mechanistic studies on cyclohexanone monooxygenase. Biochemistry. 21:1982;2644-2655.
    • (1982) Biochemistry , vol.21 , pp. 2644-2655
    • Ryerson, C.C.1    Ballou, D.P.2    Walsh, C.3
  • 16
    • 0000415356 scopus 로고
    • The enzymatic Baeyer-Villiger oxidation: Enantioselective synthesis of lactones from mesomeric cyclohexanones
    • Tachner M.J., Black D.J. The enzymatic Baeyer-Villiger oxidation. enantioselective synthesis of lactones from mesomeric cyclohexanones Journal of the American Chemical Society. 110:1988;6892-6893.
    • (1988) Journal of the American Chemical Society , vol.110 , pp. 6892-6893
    • Tachner, M.J.1    Black, D.J.2
  • 17
    • 0025123431 scopus 로고
    • Cyclohexanone 1,2-Monooxygenase from acinetobacter NCIMB 9871
    • Trudgill P.W. Cyclohexanone 1,2-Monooxygenase from acinetobacter NCIMB 9871. Methods in Enzymology. 188:1990;70-77.
    • (1990) Methods in Enzymology , vol.188 , pp. 70-77
    • Trudgill, P.W.1
  • 18
    • 84990161999 scopus 로고
    • Enzymic Baeyer-Villiger oxidations by flavin-dependant monooxygenases
    • Walsh T., Chen Y.C. Enzymic Baeyer-Villiger oxidations by flavin-dependant monooxygenases. Angew Chemistry International. 27:1988;333-343.
    • (1988) Angew Chemistry International , vol.27 , pp. 333-343
    • Walsh, T.1    Chen, Y.C.2
  • 19
    • 0031081656 scopus 로고    scopus 로고
    • Structural studies and synthetic application of Baeyer-Villiger monooxygenases
    • Willetts A. Structural studies and synthetic application of Baeyer-Villiger monooxygenases. Trends in Biotechnology. 15:1997;55-62.
    • (1997) Trends in Biotechnology , vol.15 , pp. 55-62
    • Willetts, A.1
  • 20
    • 0000999905 scopus 로고
    • Enzyme catalysed organic synthesis: NAD(P)H cofactor regeneration by using glucose-6-phosphate and the glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides
    • Wong C., Whitesides G. Enzyme catalysed organic synthesis. NAD(P)H cofactor regeneration by using glucose-6-phosphate and the glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides Journal of the American Chemical Society. 103:1981;4890-4899.
    • (1981) Journal of the American Chemical Society , vol.103 , pp. 4890-4899
    • Wong, C.1    Whitesides, G.2
  • 21
    • 0000466280 scopus 로고
    • Biotransformation reactor selection and design
    • J.M.S. Cabral, D. Best, L. Boros, & J. Tramper. Chur: Harwood Academic
    • Woodley J.M., Lilly M.D. Biotransformation reactor selection and design. Cabral J.M.S., Best D., Boros L., Tramper J. Applied Biocatalysis. 1994;371-393 Harwood Academic, Chur.
    • (1994) Applied Biocatalysis , pp. 371-393
    • Woodley, J.M.1    Lilly, M.D.2
  • 23
    • 85047677949 scopus 로고    scopus 로고
    • The use of windows of operation as a bioprocess design tool
    • Woodley J.M., Titchener-Hooker N. The use of windows of operation as a bioprocess design tool. Bioprocess Engineering. 14:1996;263-268.
    • (1996) Bioprocess Engineering , vol.14 , pp. 263-268
    • Woodley, J.M.1    Titchener-Hooker, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.