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Glycosidation of trypsin with end-group activated dextran

Paper ID Volume ID Publish Year Pages File Format Full-Text
36089 45120 2006 5 PDF Available
Title
Glycosidation of trypsin with end-group activated dextran
Abstract

A monoaminated dextran derivative was attached to trypsin via a carbodiimide-catalyzed reaction. The modified enzyme contained 3 mol of polysaccharide per mol of protein, and retained about 93% and 85% of the native esterolytic and proteolytic activity, respectively. The thermostability was enhanced from 49.7 to 67.4 °C for modified trypsin. The activation free energy of thermal inactivation at 55 °C was increased by 7.2 kJ/mol for the protease after modification with the polymer. The improved conformational stability of trypsin after glycosidation with dextran was confirmed by fluorescence spectroscopy. The glycosidated protease retained 70% of its initial activity after 3 h incubation at pH 9.0.

Keywords
Dextran; Enzyme stability; Glycosidation; Trypsin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 5, May 2006, Pages 1155–1159
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
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