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Purification and characterization of a novel NADPH-dependent 2-aminoacetophenone reductase from Arthrobacter sulfureus

Paper ID Volume ID Publish Year Pages File Format Full-Text
20325 43169 2015 4 PDF Available
Title
Purification and characterization of a novel NADPH-dependent 2-aminoacetophenone reductase from Arthrobacter sulfureus
Abstract

A novel 2-aminoacetophenone reductase was purified to homogeneity from Arthrobacter sulfureus BW1010. The enzyme is a monomer with a molecular weight of approximately 60 kDa. Using NADPH as coenzyme, it catalyzes the reduction of ketones, especially amine phenyl ketones, and stereospecifically reduces 2-aminoacetophenone to (S)-2-amino-1-phenylethanol (e.e > 99.8%) with the optimal pH at 7.5.

Keywords
2-Aminoacetophenone reductase; (S)-2-Amino-1-phenylethanol; Arthrobacter sulfureus; Reduction; NADPH-dependent
First Page Preview
Purification and characterization of a novel NADPH-dependent 2-aminoacetophenone reductase from Arthrobacter sulfureus
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 119, Issue 6, June 2015, Pages 648–651
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering