Comparison of cyclohexanone monooxygenase as an isolated enzyme and whole cell biocatalyst for the enantioselective oxidation of 1,3-dithiane (Articolo in rivista)

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Label
  • Comparison of cyclohexanone monooxygenase as an isolated enzyme and whole cell biocatalyst for the enantioselective oxidation of 1,3-dithiane (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.molcatb.2004.09.005 (literal)
Alternative label
  • Zambianchi F.(1); Raimondi S.(1); Pasta P.(1); Carrea G. (1); Gaggero N.(2); Woodley J.M. (3) (2004)
    Comparison of cyclohexanone monooxygenase as an isolated enzyme and whole cell biocatalyst for the enantioselective oxidation of 1,3-dithiane
    in Journal of molecular catalysis. B, Enzymatic (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Zambianchi F.(1); Raimondi S.(1); Pasta P.(1); Carrea G. (1); Gaggero N.(2); Woodley J.M. (3) (literal)
Pagina inizio
  • 165 (literal)
Pagina fine
  • 171 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.sciencedirect.com/science/article/pii/S1381117704002437 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 31 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • (1) Istituto di Chimica del Riconoscimento Molecolare-CNR, Via Mario Bianco 9, 20131 Milano, Italy (2) Istituto di Chimica Organica Alessandro Marchesini, Facoltà di Farmacia, Via Venezian 21, 20133 Milano, Italy (3) Department of Biochemical Engineering, University College London, Torrington Place, London WC1E 7JE, UK (literal)
Titolo
  • Comparison of cyclohexanone monooxygenase as an isolated enzyme and whole cell biocatalyst for the enantioselective oxidation of 1,3-dithiane (literal)
Abstract
  • Both whole cells of recombinant Escherichia coli TOP10, overexpressing cyclohexanone monooxygenase (CHMO) and isolated cyclohexanone monooxygenase, were used to carry out the enantioselective oxidation of 1,3-dithiane (1) to (R)-1,3-dithiane-1-oxide (2). The two biocatalysts were evaluated under various experimental conditions (e.g., shaken flask or bioreactor; non-bound or resin-adsorbed substrate; different substrate concentrations) in terms of volumetric productivity and enantioselectivity. While productivity was similar in the two cases (up to 0.58 g L-1 h-1), the optical purity of the product was much higher with the isolated enzyme (up to 98% e.e.) than with the whole cell biocatalyst (up to 85% e.e.). (literal)
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