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Characterization of d-galacturonate reductase purified from the psychrophilic yeast species Cryptococcus diffluens

Paper ID Volume ID Publish Year Pages File Format Full-Text
21282 43215 2011 4 PDF Available
Title
Characterization of d-galacturonate reductase purified from the psychrophilic yeast species Cryptococcus diffluens
Abstract

d-Galacturonic acid reductase was purified from a psychrophilic yeast strain of Cryptococcus diffluens, which was isolated from Satho, a traditional alcohol drink in Thailand. This enzyme, named Cd-GalUAR, assimilates d-galacturonic acid and requires NADPH as a cofactor. Cd-GalUAR is about 45 kDa and stable from pH 6.5 to 7.5 and up to 35°C. Its optimum pH and temperature are pH 7.0 and 40°C, respectively. However, 80% of its maximum activity remained at 4°C. The reaction of Cd-GalUAR from d-galacturonic acid produces L-galactonic acid, which was identified by 13C NMR and LC–MS. Three amino acid sequences were determined from trypsin-digested peptides of Cd-GalUAR. Similar sequences are found in many NAD or NADP oxidoreductases, including some d-galacturonate reductases. Our results suggest that Cd-GalUAR is the first d-galacturonate reductase identified in yeast.

Keywords
Galacturonate reductase; Psychrophilic yeast; Cryptococcus diffluens; Enzymatic characterization
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Characterization of d-galacturonate reductase purified from the psychrophilic yeast species Cryptococcus diffluens
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 111, Issue 5, May 2011, Pages 518–521
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