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Volumn 53, Issue 4, 2013, Pages 283-287

A self-sufficient Baeyer-Villiger biocatalysis system for the synthesis of ε-caprolactone from cyclohexanol

Author keywords

Caprolactone; Baeyer Villiger monooxygenase; Biocatalysis; Co immobilization; Cofactor recycling

Indexed keywords

BAEYER-VILLIGER MONOOXYGENASES; BIOCATALYSIS; CAPROLACTONE; CO-FACTOR RECYCLING; COIMMOBILIZATION;

EID: 84881555309     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.01.007     Document Type: Article
Times cited : (80)

References (29)
  • 2
    • 84856717640 scopus 로고    scopus 로고
    • Expanding the organic toolbox: a guide to integrating biocatalysis in synthesis
    • Clouthier C.M., Pelletier J.N. Expanding the organic toolbox: a guide to integrating biocatalysis in synthesis. Chemical Society Reviews 2012, 41:1585-1605.
    • (2012) Chemical Society Reviews , vol.41 , pp. 1585-1605
    • Clouthier, C.M.1    Pelletier, J.N.2
  • 8
    • 0017227971 scopus 로고
    • The purification and properties of cyclohexanone oxygenase from Nocardia globerula CL1 and Acinetobacter NCIB 9871
    • Donoghue N.A., Norris D.B., Trudgill P.W. The purification and properties of cyclohexanone oxygenase from Nocardia globerula CL1 and Acinetobacter NCIB 9871. European Journal of Biochemistry 1976, 63:175-192.
    • (1976) European Journal of Biochemistry , vol.63 , pp. 175-192
    • Donoghue, N.A.1    Norris, D.B.2    Trudgill, P.W.3
  • 9
    • 0023958999 scopus 로고
    • Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence determination
    • Chen Y.C., Peoples O.P., Walsh C.T. Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence determination. Journal of Bacteriology 1988, 170:781-789.
    • (1988) Journal of Bacteriology , vol.170 , pp. 781-789
    • Chen, Y.C.1    Peoples, O.P.2    Walsh, C.T.3
  • 10
    • 84990161999 scopus 로고
    • Enzymic Baeyer-Villiger oxidations by flavin-dependent monooxygenases
    • Walsh C.T., Chen Y.C. Enzymic Baeyer-Villiger oxidations by flavin-dependent monooxygenases. Angewandte Chemie International Edition 1988, 27:333-343.
    • (1988) Angewandte Chemie International Edition , vol.27 , pp. 333-343
    • Walsh, C.T.1    Chen, Y.C.2
  • 11
    • 78049304724 scopus 로고    scopus 로고
    • Recent developments in the application of Baeyer-Villiger monooxygenases as biocatalysts
    • de Gonzalo G., Mihovilovic M.D., Fraaije M.W. Recent developments in the application of Baeyer-Villiger monooxygenases as biocatalysts. ChemBioChem 2010, 11:2208-2231.
    • (2010) ChemBioChem , vol.11 , pp. 2208-2231
    • de Gonzalo, G.1    Mihovilovic, M.D.2    Fraaije, M.W.3
  • 12
    • 0031838334 scopus 로고    scopus 로고
    • Cyclohexanone monooxygenase: a useful reagent for asymmetric Baeyer-Villiger reactions
    • Stewart J.D. Cyclohexanone monooxygenase: a useful reagent for asymmetric Baeyer-Villiger reactions. Current Organic Chemistry 1998, 2:195-216.
    • (1998) Current Organic Chemistry , vol.2 , pp. 195-216
    • Stewart, J.D.1
  • 14
    • 34547114478 scopus 로고    scopus 로고
    • Enhanced production of ε-caprolactone by overexpression of NADPH-regenerating glucose 6-phosphate dehydrogenase in recombinant Escherichia coli harboring cyclohexanone monooxygenase gene
    • Lee W-H., Park J-B., Park K., Kim M-D., Seo J-H. Enhanced production of ε-caprolactone by overexpression of NADPH-regenerating glucose 6-phosphate dehydrogenase in recombinant Escherichia coli harboring cyclohexanone monooxygenase gene. Applied Microbiology and Biotechnology 2007, 76:329-338.
    • (2007) Applied Microbiology and Biotechnology , vol.76 , pp. 329-338
    • Lee, W.-H.1    Park, J.-B.2    Park, K.3    Kim, M.-D.4    Seo, J.-H.5
  • 15
    • 78649899395 scopus 로고    scopus 로고
    • Enzymatic and whole cell catalysis: finding new strategies for old processes
    • de Carvalho C.C.C.R. Enzymatic and whole cell catalysis: finding new strategies for old processes. Biotechnology Advances 2011, 29:75-83.
    • (2011) Biotechnology Advances , vol.29 , pp. 75-83
    • de Carvalho, C.C.C.R.1
  • 17
    • 77349127553 scopus 로고    scopus 로고
    • Monooxygenases as biocatalysts: classification, mechanistic aspects and biotechnological applications
    • Torres Pazmiño D.E., Winkler M., Glieder A., Fraaije M.W. Monooxygenases as biocatalysts: classification, mechanistic aspects and biotechnological applications. Journal of Biotechnology 2010, 146:9-24.
    • (2010) Journal of Biotechnology , vol.146 , pp. 9-24
    • Torres Pazmiño, D.E.1    Winkler, M.2    Glieder, A.3    Fraaije, M.W.4
  • 21
    • 84863953159 scopus 로고    scopus 로고
    • Discovery, application and protein engineering of Baeyer-Villiger monooxygenases for organic synthesis
    • Balke K., Kadow M., Mallin H., Saß S., Bornscheuer U.T. Discovery, application and protein engineering of Baeyer-Villiger monooxygenases for organic synthesis. Organic and Biomolecular Chemistry 2012, 10:6249.
    • (2012) Organic and Biomolecular Chemistry , vol.10 , pp. 6249
    • Balke, K.1    Kadow, M.2    Mallin, H.3    Saß, S.4    Bornscheuer, U.T.5
  • 24
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier F.W. Protein production by auto-induction in high-density shaking cultures. Protein Expression and Purification 2005, 41:207-234.
    • (2005) Protein Expression and Purification , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 25
    • 80054898961 scopus 로고    scopus 로고
    • Kinetic resolution of glyceraldehyde using an aldehyde dehydrogenase from Deinococcus geothermalis DSM 11300 combined with electrochemical cofactor recycling
    • Wulf H., Perzborn M., Sievers G., Scholz F., Bornscheuer U.T. Kinetic resolution of glyceraldehyde using an aldehyde dehydrogenase from Deinococcus geothermalis DSM 11300 combined with electrochemical cofactor recycling. Journal of Molecular Catalysis B: Enzymatic 2012, 74:144-150.
    • (2012) Journal of Molecular Catalysis B: Enzymatic , vol.74 , pp. 144-150
    • Wulf, H.1    Perzborn, M.2    Sievers, G.3    Scholz, F.4    Bornscheuer, U.T.5
  • 28
    • 0020909885 scopus 로고
    • Immobilization of glucose oxidase on montmorillonite clay: hydrophobic and ionic modes of binding
    • Garwood G.A., Mortland M.M., Pinnavaia T.J. Immobilization of glucose oxidase on montmorillonite clay: hydrophobic and ionic modes of binding. Journal of Molecular Catalysis 1983, 22:153-163.
    • (1983) Journal of Molecular Catalysis , vol.22 , pp. 153-163
    • Garwood, G.A.1    Mortland, M.M.2    Pinnavaia, T.J.3
  • 29
    • 38349156041 scopus 로고    scopus 로고
    • Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase
    • Forneris F., Heuts D.P.H.M., Delvecchio M., Rovida S., Fraaije M.W., Mattevi A. Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase. Biochemistry 2008, 47:978-985.
    • (2008) Biochemistry , vol.47 , pp. 978-985
    • Forneris, F.1    Heuts, D.P.H.M.2    Delvecchio, M.3    Rovida, S.4    Fraaije, M.W.5    Mattevi, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.