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Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose

Paper ID Volume ID Publish Year Pages File Format Full-Text
25239 43562 2006 10 PDF Available
Title
Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose
Abstract

Immobilization of alcohol dehydrogenase (ADH) from Horse Liver inside porous supports promotes a dramatic stabilization of the enzyme against inactivation by air bubbles in stirred tank reactors. Moreover, immobilization of ADH on glyoxyl-agarose promotes additional stabilization against any distorting agent (pH, temperature, organic solvents, etc.). Stabilization is higher when using highly activated supports, they are able to immobilize both subunits of the enzyme. The best glyoxyl derivatives are much more stable than conventional ADH derivatives (e.g., immobilized on BrCN activated agarose). For example, glyoxyl immobilized ADH preserved full activity after incubation at pH 5.0 for 20 h at room temperature and conventional derivatives (as well as the soluble enzyme) preserved less than 50% of activity after incubation under the same conditions. Moreover, glyoxyl derivatives are more than 10 times more stable than BrCN derivatives when incubated in 50% acetone at pH 7.0. Multipoint covalent immobilization, in addition to multisubunit immobilization, seems to play an important stabilizing role against distorting agents. In spite of these interesting stabilization factors, immobilization hardly promotes losses of catalytic activity (keeping values near to 90%). This immobilized preparation is able to keep good activity using dextran-NAD+. In this way, ADH glyoxyl immobilized preparation seems to be suitable to be used as cofactor-recycling enzyme-system in interesting NAD+-mediated oxidation processes, catalyzed by other immobilized dehydrogenases in stirred tank reactors.

Keywords
Enzyme redox reactions; Cofactor regeneration; Inactivation by gas bubbles; Enzyme rigidification; Stabilization of multimeric enzymes
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Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 125, Issue 1, 20 August 2006, Pages 85–94
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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