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Glycosidation of phenylalanine dehydrogenase with O-carboxymethyl-poly-β-cyclodextrin

Paper ID Volume ID Publish Year Pages File Format Full-Text
18381 42720 2007 5 PDF Available
Title
Glycosidation of phenylalanine dehydrogenase with O-carboxymethyl-poly-β-cyclodextrin
Abstract

The polysaccharide O-carboxymethyl poly-β-cyclodextrin (M = 1.3 × 104, 40% COOH groups) was employed as modification agent for Bacillus badius phenylalanine dehydrogenase via a carbodiimide-catalyzed reaction. The neoglycoenzyme retained 63% of its initial activity and contained about 2.5 mol of polymer per mole of enzyme. The optimum temperature for the enzyme was increased by 15 °C and its thermostability was improved by about 6 °C over 10 min incubation. The conjugate was also more resistant to thermal inactivation at different temperatures, ranging from 45 to 60 °C. The improved conformational stability of the modified enzyme was confirmed by fluorescence spectroscopy.

Keywords
Phenylalanine dehydrogenase; Cyclodextrin; Enzyme stability; Glycosidation
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Glycosidation of phenylalanine dehydrogenase with O-carboxymethyl-poly-β-cyclodextrin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 40, Issue 3, 5 February 2007, Pages 471–475
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