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Thermostabilization of Bacillus amyloliquefaciens α-amylase by chemical cross-linking

Paper ID Volume ID Publish Year Pages File Format Full-Text
25530 43579 2006 9 PDF Available
Title
Thermostabilization of Bacillus amyloliquefaciens α-amylase by chemical cross-linking
Abstract

Chemical cross-linking of a mesophilic α-amylase from Bacillus amyloliquefaciens (BAA) was carried out. Intra-molecular cross-links between lysine residues upon treatment of the enzyme with ethylene glycol bis(succinic acid N-hydroxy succinimide ester) resulted in enhancement of thermostability as indicated by irreversible thermoinactivation experiments. Enhancement of thermostability coincided with a dramatic protection against aggregation, combined with a decrease in surface hydrophobicity. Deamidation, another important mechanism of irreversible thermoinactivation, was also diminished upon modification. While no significant changes in the kinetic parameters are evident, rigidification of the protein structure is suggested by circular dichroism (CD) and fluorescence studies.

Keywords
α-Amylase; Chemical cross-linking; Thermostability; Aggregation; Hydrophobicity; Deamidation
First Page Preview
Thermostabilization of Bacillus amyloliquefaciens α-amylase by chemical cross-linking
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 123, Issue 4, 10 June 2006, Pages 434–442
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering