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Titolo:
Challenges in capturing oxygenase activity in vitro
Autore:
Vilker, VL; Reipa, V; Mayhew, M; Holden, MJ;
Indirizzi:
Natl Inst Stand & Technol, Div Biotechnol, Gaithersburg, MD 20899 USA NatlInst Stand & Technol Gaithersburg MD USA 20899 ersburg, MD 20899 USA
Titolo Testata:
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
fascicolo: 11, volume: 76, anno: 1999,
pagine: 1283 - 1289
SICI:
0003-021X(199911)76:11<1283:CICOAI>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIRECT ELECTRON-TRANSFER; MODIFIED GOLD ELECTRODE; CYTOCHROME-C; ENZYMATIC REDUCTION; SILVER ELECTRODE; DIRECT ELECTROCHEMISTRY; INSITU REGENERATION; ORGANIC-SYNTHESIS; MEMBRANE REACTOR; PUTIDAREDOXIN;
Keywords:
biocatalysis; bioelectrochemistry; cytochrome P450; desaturase; electro-enzymology; 5-exo-hydroxy camphor; omega-hydroxylation of fatty acids; monooxygenase; NAD(P)H regeneration; styrene oxide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Vilker, VL Natl Inst Stand & Technol, Div Biotechnol, Gaithersburg, MD 20899 USA Natl Inst Stand & Technol Gaithersburg MD USA 20899 20899 USA
Citazione:
V.L. Vilker et al., "Challenges in capturing oxygenase activity in vitro", J AM OIL CH, 76(11), 1999, pp. 1283-1289

Abstract

Biocatalysis using oxygenase or desaturase enzymes has the potential to add value to native fats and oils by adding oxygen, hydroxyl groups, or double bonds to create regio- and/or stereospecific products. These enzymes are a subset of the large class of oxidoreductase enzymes (from EC subgroups 1.13 and 1.14) involved with biological oxidation and reduction. In vitro biocatalytic processing using these enzymes is hampered by the high cost of the stoichiometric cofactors. This article reviews recent progress in developing in vitro redox enzyme biocatalysis for commercial-scale syntheses. Coenzyme recycling and electrochemical redox cycling as methods for cofactor regeneration are described and commercial applications indicated. Direct charge transfer without use of mediators is described as the cleanest way of introducing the reducing power into the catalytic cycle. Our electrochemically driven cytochrome P450(cam) bioreactor is discussed as an example of direct charge transfer to a redox protein. Site-directed mutagenesis in the active site of the P450(cam) monooxygenase greatly improved performance for the conversion of the nonnative substrate, styrene to styrene oxide. This epoxidation reaction was also shown to give a single product (styrene oxide) in the bioelectrochemical reactor when the diatomic oxygen co-substrate was managed properly.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 10:10:15