6033-23-4Relevant articles and documents
Co-immobilized Whole Cells with ω-Transaminase and Ketoreductase Activities for Continuous-Flow Cascade Reactions
Nagy-Gy?r, László,Abaházi, Emese,Bódai, Viktória,Sátorhelyi, Péter,Erdélyi, Balázs,Balogh-Weiser, Diána,Paizs, Csaba,Hornyánszky, Gábor,Poppe, László
, p. 1845 - 1848 (2018/09/10)
An improved sol–gel process involving the use of hollow silica microspheres as a supporting additive was applied for the co-immobilization of whole cells of Escherichia coli with Chromobacterium violaceum ω-transaminase activity and Lodderomyces elongisporus with ketoreductase activity. The co-immobilized cells with two different biocatalytic activities could perform a cascade of reactions to convert racemic 4-phenylbutan-2-amine or heptan-2-amine into a nearly equimolar mixture of the corresponding enantiomerically pure R amine and S alcohol even in continuous-flow mode. The novel co-immobilized whole-cell system proved to be an easy-to-store and durable biocatalyst.
ALKANE OXIDATION BY MODIFIED HYDROXYLASES
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Paragraph 0323; 0324, (2016/02/16)
This invention relates to modified hydroxylases. The invention further relates to cells expressing such modified hydroxylases and methods of producing hydroxylated alkanes by contacting a suitable substrate with such cells.
A novel P450-based biocatalyst for the selective production of chiral 2-alkanols
Von Bühler, Clemens J.,Urlacher, Vlada B.
supporting information, p. 4089 - 4091 (2014/04/03)
A P450 monooxygenase from Nocardia farcinica (CYP154A8) catalyses the stereo- and regioselective hydroxylation of n-alkanes, still a challenging task in chemical catalysis. In a biphasic reaction system, the regioselectivity for the C2-position of C7-C9 alkanes was over 90%. The enzyme showed strict S-selectivity for all tested substrates, with enantiomeric excess (ee) of up to 91%. This journal is the Partner Organisations 2014.