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Different mechanisms of protein immobilization on glutaraldehyde activated supports: Effect of support activation and immobilization conditions

Paper ID Volume ID Publish Year Pages File Format Full-Text
18535 42725 2006 6 PDF Available
Title
Different mechanisms of protein immobilization on glutaraldehyde activated supports: Effect of support activation and immobilization conditions
Abstract

The precise control of the conditions during support activation with glutaraldehyde has enabled the modification of the amino groups of the matrix with one or two glutaraldehyde molecules. Moreover, the use of aminated supports implies that below each glutaraldehyde molecule, there are amino groups and, therefore, these supports could be considered as heterofunctional matrices; an anion exchanger bearing glutaraldehyde groups for covalent immobilization.Thus, by using several enzymes as models, it has been found that at low ionic strength the protein immobilization on glutaraldehyde activated supports proceeds via a first ionic interchange of the protein on the amino groups of the support, followed by the covalent reaction. Moreover, the dimeric form of glutaraldehyde seems to be much more reactive than its monomeric counterpart, permitting the immobilization of proteins even at very high ionic strength. Although in all cases the immobilization of the enzymes on both monomer and dimeric matrices promoted a significant increment in the enzyme stability, it was found that the stabilization depends on the degree of activation (monomer or dimer), and it is necessary to analyze each individual enzyme before selecting any of the immobilization protocols.

Keywords
Glutaraldehyde; Hetero-functional supports; Physical adsorption of proteins; Covalent immobilization of proteins; Protein stabilization
First Page Preview
Different mechanisms of protein immobilization on glutaraldehyde activated supports: Effect of support activation and immobilization conditions
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 4, 2 August 2006, Pages 877–882
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering