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Gas phase enantioselective reduction catalyzed by immobilized ketoreductase: Effects of water activity and reaction temperature

Paper ID Volume ID Publish Year Pages File Format Full-Text
3904 197 2010 3 PDF Available
Title
Gas phase enantioselective reduction catalyzed by immobilized ketoreductase: Effects of water activity and reaction temperature
Abstract

The performance (activity, stability, enantioselectivity and productivity) of the commercial ketoreductase immobilized on non-porous glass supports was investigated as functions of the water activity and the reaction temperature in a continuous gas phase reactor. The enantioselective reduction of 2-butanone to (S)-2-butanol with the in situ regeneration of β-nicotinamide adenine dinucleotide phosphate by 2-propanol catalyzed by the immobilized ketoreductase was used as a model reaction. The activity, stability and enantioselectivity were strongly influenced by the water activity and the reaction temperature. The optimal water activity and reaction temperature were obtained at 0.8 and 313–323 K in terms of the productivity, respectively. Successfully, the enantioselectivity for the gas phase system attained the level identical to that for the aqueous phase system.

Keywords
Biocatalysis; Gas phase; Ketoreductase; Immobilization; Reduction; Enantioselectivity
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Gas phase enantioselective reduction catalyzed by immobilized ketoreductase: Effects of water activity and reaction temperature
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 52, Issues 2–3, 15 November 2010, Pages 301–303
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Full-text PDF Download
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