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Characterization of an exocellular β-glucosidase from Debaryomyces pseudopolymorphus

Paper ID Volume ID Publish Year Pages File Format Full-Text
18316 42718 2006 6 PDF Available
Title
Characterization of an exocellular β-glucosidase from Debaryomyces pseudopolymorphus
Abstract

When grown in complex media containing 20 g of cellobiose per litre, Debaryomyces pseudopolymorphus secreted a β-glucosidase. The synthesis of this enzyme was repressed by glucose. Most of the enzyme was concentrated in the supernatant, with only 10% of the total activity being cell associated. This β-glucosidase (designated Dp-βgl) was purified and shown to be a monomer with a native molecular mass of approximately 100,000 Da. It demonstrated optimal activity at a pH of 4 and, in the short term (no more than 2 h), at a temperature of 40 °C. Temperature-stability analysis revealed that the enzyme was labile at 50 °C and above. It had a strong affinity for cellobiose and maltose, and degraded laminarin. It was inhibited by Ca++, Zn++, Mg++ and acetic acid, but apparently not by glucose and ethanol.

Keywords
β-Glucosidase; Debaryomyces pseudopolymorphus; Exocellular; Glucose resistance; Wine aroma
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Characterization of an exocellular β-glucosidase from Debaryomyces pseudopolymorphus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 2, 26 June 2006, Pages 229–234
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
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Price after discount Only $4.95
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Full-text PDF Download
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