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Molecules 2014, 19(7), 8995-9018; doi:10.3390/molecules19078995
Review

Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases

* ,
 and
University of Silesia in Katowice, Faculty of Biology and Environmental Protection, Department of Biochemistry, Jagiellonska 28, 40-032 Katowice, Poland
* Author to whom correspondence should be addressed.
Received: 12 May 2014 / Revised: 13 June 2014 / Accepted: 16 June 2014 / Published: 27 June 2014
(This article belongs to the Special Issue Enzyme Immobilization)
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Abstract

The main objective of the immobilization of enzymes is to enhance the economics of biocatalytic processes. Immobilization allows one to re-use the enzyme for an extended period of time and enables easier separation of the catalyst from the product. Additionally, immobilization improves many properties of enzymes such as performance in organic solvents, pH tolerance, heat stability or the functional stability. Increasing the structural rigidity of the protein and stabilization of multimeric enzymes which prevents dissociation-related inactivation. In the last decade, several papers about immobilization methods have been published. In our work, we present a relation between the influence of immobilization on the improvement of the properties of selected oxidoreductases and their commercial value. We also present our view on the role that different immobilization methods play in the reduction of enzyme inhibition during biotechnological processes.
Keywords: oxidoreductases; immobilization; stability of enzyme oxidoreductases; immobilization; stability of enzyme
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Guzik, U.; Hupert-Kocurek, K.; Wojcieszyńska, D. Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases. Molecules 2014, 19, 8995-9018.

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