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Stabilization of α-chymotrypsin by chemical modification with monoamine cyclodextrin

Paper ID Volume ID Publish Year Pages File Format Full-Text
36689 45142 2005 4 PDF Available
Title
Stabilization of α-chymotrypsin by chemical modification with monoamine cyclodextrin
Abstract

Bovine pancreatic α-chymotrypsin was chemically modified with mono-6-amino-6-deoxy-β-cyclodextrin. The modified enzymes contained about 2 mol of oligosaccharide per mol of protein and retained full proteolytic and esterasic activity. The optimum temperature for α-chymotrypsin was increased by 5 °C and its thermostability was enhanced by about 6 °C after modification. The glycosylated enzyme turned markedly more resistant to thermal inactivation at 50 °C and retained 70% of the original activity when pre-incubated at pH 9.0 for 180 min as compared to a complete inactivation seed for the unmodified protease.

Keywords
α-Chymotrypsin; Aminated β-cyclodextrin; Modified enzyme; Enzyme stability
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Stabilization of α-chymotrypsin by chemical modification with monoamine cyclodextrin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 40, Issue 6, May 2005, Pages 2091–2094
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
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Full-text PDF Download
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