http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17428
Biocatalytic properties of Baeyer-Villiger monooxygenases in aqueous-organic media (Articolo in rivista)
- Type
- Label
- Biocatalytic properties of Baeyer-Villiger monooxygenases in aqueous-organic media (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.molcatb.2006.01.010 (literal)
- Alternative label
Gonzalo D.G., Ottolina G., Zambianchi F., Fraaije M.W., Carrea G. (2006)
Biocatalytic properties of Baeyer-Villiger monooxygenases in aqueous-organic media
in Journal of molecular catalysis. B, Enzymatic (Print); ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS, AMSTERDAM (Paesi Bassi)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Gonzalo D.G., Ottolina G., Zambianchi F., Fraaije M.W., Carrea G. (literal)
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- http://www.sciencedirect.com/science/article/pii/S1381117706000282 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Chimica del Riconoscimento Molecolare, CNR, via Mario Bianco 9, 20131 Milano, Italy
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, (literal)
- Titolo
- Biocatalytic properties of Baeyer-Villiger monooxygenases in aqueous-organic media (literal)
- Abstract
- The biocatalytic properties of three Baeyer-Villiger monooxygenases (phenylacetone monooxygenase, 4-hydroxyacetophenone monooxygenase and ethionamide monooxygenase) in a variety of aqueous-organic media were studied using organic sulfides as substrates. The influence of the nature and the concentration of the solvents, as well as of the substrates, on the activity and enantioselectivity of the enzymes was investigated in detail. Solvents were found to decrease, to a different extent, enzyme activity. High increases of enantioselectivity and also reversal of enantiopreference were observed depending on the enzyme and on the nature of the solvent and the substrate employed. (literal)
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