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Stabilization of the quaternary structure of a hexameric alpha-galactosidase from Thermus sp. T2 by immobilization and post-immobilization techniques

Paper ID Volume ID Publish Year Pages File Format Full-Text
35592 45097 2008 6 PDF Available
Title
Stabilization of the quaternary structure of a hexameric alpha-galactosidase from Thermus sp. T2 by immobilization and post-immobilization techniques
Abstract

An alpha-galactosidase from Thermus sp. T2, a hexameric protein, has been immobilized on cyanogen bromide agarose, retaining its activity almost intact, but without any significant improvement in enzyme stability. In fact, enzyme subunits could be desorbed from the immobilized preparation by boiling the solution in the presence of SDS (detected by SDS-PAGE) and a dependence of the enzyme stability on the enzyme concentration could be detected under certain conditions. The further cross-linking of this immobilized preparation with aldehyde–dextran permitted to improve the enzyme stability, avoiding the release of enzyme subunits to the reaction medium that could produce enzyme inactivation or food contamination.

Keywords
Multimeric enzymes; Enzyme stabilization; Cross-linking; Aldehyde–dextran
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Stabilization of the quaternary structure of a hexameric alpha-galactosidase from Thermus sp. T2 by immobilization and post-immobilization techniques
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 2, February 2008, Pages 193–198
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
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