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Purification and characterization of piceid-β-d-glucosidase from Aspergillus oryzae

Paper ID Volume ID Publish Year Pages File Format Full-Text
36319 45128 2007 6 PDF Available
Title
Purification and characterization of piceid-β-d-glucosidase from Aspergillus oryzae
Abstract

The piceid-β-d-glucosidase that hydrolyzes the β-d-glucopyranoside bond of piceid to release resveratrol was isolated from Aspergillus oryzae sp.100 strain, and the enzyme was purified and characterized. The enzyme was purified to one spot in SDS polyacrylamide gel electrophoresis, and its molecular weight was about 77 kDa. The optimum temperature of the piceid-β-d-glucosidase was 60 °C, and the optimum pH was 5.0. The piceid-β-d-glucosidase was stable at less than 60 °C, and pH 4.0–5.0. Ca2+, Mg2+ and Zn2+ ions have no significant effect on enzyme activity, but Cu2+ ion inhibits enzyme activity strongly. The Km value was 0.74 mM and the Vmax value was 323 nkat mg−1 for piceid.

Keywords
Purification; Characterization; Piceid-β-d-glucosidase; Aspergillus oryzae; Resveratrol
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 42, Issue 1, January 2007, Pages 83–88
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
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Any Questions? feel free to contact us