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Purification and characterization of fluorinated ketone reductase from Geotrichum candidum NBRC 5767

Paper ID Volume ID Publish Year Pages File Format Full-Text
3389 167 2013 4 PDF Available
Title
Purification and characterization of fluorinated ketone reductase from Geotrichum candidum NBRC 5767
Abstract

•We successfully purified and characterized the fluorinated ketone reductase from Geotrichum candidum NBRC 5767.•The fluorinated ketone reductase is highly selective for α fluorinated ketones.•The fluorinated ketone reductase from G. candidum NBRC 5767 is unique and can be used in the synthesis of optically pure fluorinated alcohols.

Biocatalysts that can specifically catalyze the transformations of fluorinated compounds are rare. A novel NADPH-dependent fluorinated ketone reductase that reduces trifluoroacetophenone to (S)-trifluorophenylethanol with excellent enantioselectivity (ee > 99%) from Geotrichum candidum NBRC 5767 was isolated, purified, and characterized. Through ammonium sulfate fractionation and several chromatographies, this enzyme was purified to 95-fold with 3.5% yield. Gel filtration chromatography with SDS-PAGE revealed this protein to be a dimer of 60 kDa subunits. An investigation of the substrate specificity of the purified enzyme revealed that it was highly selective for ketones containing fluorines at the α position.

Keywords
Enzymes; Biocatalysis; Purification; Enantioseparation; Trifluoroacetophenone; Asymmetric reduction
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Purification and characterization of fluorinated ketone reductase from Geotrichum candidum NBRC 5767
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 76, 15 July 2013, Pages 13–16
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
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us