Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6491293 | Journal of Biotechnology | 2014 | 7 Pages |
Abstract
An artificial enzyme cascade composed of an alcohol dehydrogenase, an enoate reductase and a Baeyer-Villiger monooxygenase was investigated in vitro to gain deeper mechanistic insights and understand the assets and drawbacks of this multi-step biocatalysis. Several substrates composed of different structural motifs were examined and provided access to functionalized chiral compounds in high yields (up to >99%) and optical purities (up to >99%). Hence, the applicability of the presented enzymatic cascade was exploited for the synthesis of biorenewable polyesters.
Keywords
Cyclohexanone monooxygenaseG6PBVMOBaeyer–Villiger monooxygenasePMSFADHNADPHIPTGCHMOCFEG6P-DHEnoate reductaseNAD+NADP+SDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisAlcohol dehydrogenaseisopropyl-β-d-thiogalactopyranosideterrific brothcell free extractphenylmethylsulfonyl fluoridelysogeny brothNADHnicotinamide adenine dinucleotidenicotinamide adenine dinucleotide (reduced)nicotinamide adenine dinucleotide phosphatenicotinamide adenine dinucleotide phosphate (reduced)optical densityGas chromatographyGlucose 6-phosphateglucose 6-phosphate dehydrogenase
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Nikolin Oberleitner, Christin Peters, Florian Rudroff, Uwe T. Bornscheuer, Marko D. Mihovilovic,