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Purification, characterization and molecular docking study of NADPH dependent xylose reductase from thermotolerant Kluyveromyces sp. IIPE453

Paper ID Volume ID Publish Year Pages File Format Full-Text
34245 45011 2016 10 PDF Available
Title
Purification, characterization and molecular docking study of NADPH dependent xylose reductase from thermotolerant Kluyveromyces sp. IIPE453
Abstract

•The key enzyme for xylose reduction, xylose reductase was isolated from thermotolerant Kluyveromyces sp. IIPE453 and characterized.•Enzyme was selective to NADPH as cofactor for xylose reduction with high affinity•A 3D homology model was predicted based on a related template•Molecular Docking analysis revealed tetrad of amino acid residues involved in catalytic mechanism.

A NADPH dependent xylose reductase, key enzyme for reducing xylose into xylitol, was isolated from thermotolerant yeast Kluyveromyces sp. IIPE453 and characterized in detail. Purified enzyme (37 KDa) demonstrated maximum activity in pH 6.5 and 45 °C temperature. Molecular docking study of in silico protein model revealed a set of polar amino acid residues involved in catalytic mechanism.

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Keywords
Xylose reductase; Kluyveromyces; Docking; Xylitol; Lignocellulosic biomass
First Page Preview
Purification, characterization and molecular docking study of NADPH dependent xylose reductase from thermotolerant Kluyveromyces sp. IIPE453
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 51, Issue 1, January 2016, Pages 124–133
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering