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Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins

Paper ID Volume ID Publish Year Pages File Format Full-Text
18321 42718 2006 7 PDF Available
Title
Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins
Abstract

Glyoxyl agarose is constituted by quite thick agarose fibres containing a large number of very stable aldehyde groups attached to the support by very short spacer arms. Under alkaline conditions, these activated supports immobilize proteins, via, at least, a two-point reaction involving the region/s of the protein surface with the higher densities of amino groups. These bonds are weak Schiff's bases and the reversibility of the bonds has been used to convert this matrix into a chromatographic one. A more intense multipoint attachment between the immobilized protein and the activated support can be further promoted, with minimal loss of catalytic activity, by a long-term incubation of the protein–support conjugate under suitable conditions. The end-point of the preparation of agarose–protein conjugates is a very mild borohydride reduction. After that reduction, the enzyme remains attached to the support by means of very stable secondary amino bonds (with very similar physical properties to those of the former primary amino ones) and the remaining aldehyde groups on the support are converted into fully inert hydroxyl groups. Very active and highly stabilized derivatives of many enzymes and proteins have been prepared using these supports. The main features of these protein immobilization protocols are discussed here.

Keywords
Enzyme stabilization; Enzyme purification; Multipoint covalent attachment; Enzyme rigidification; Auto-direcetd immobilization; Reductive amination; Glyoxyl agarose
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Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 2, 26 June 2006, Pages 274–280
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
Any Questions? feel free to contact us