Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review
American Journal of Chemical Engineering
Volume 5, Issue 6, November 2017, Pages: 135-139
Received: Sep. 13, 2017; Accepted: Sep. 26, 2017; Published: Nov. 13, 2017
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Authors
Abubakar Muhammad Nazif, Department of Biotechnology, Modibbo Adama University of Technology, Yola, Nigeria
Ayuba Yohanna Musa, Department of Chemistry, Abubakar Tafawa Balewa University, Bauchi, Nigeria
Muhammad Muawiya Alkali, Department of Biochemistry, Modibbo Adama University of Technology, Yola, Nigeria
Ilesanmi Esther, Department of Chemistry, University of Benin, Benin, Nigeria
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Abstract
Indigenous enzymes found in nature have found wide application in industries ascribable to their ability to catalyze complex chemical processes under moderate experimental and environmental conditions. However, the use of indigenous enzymes is yet to achieve the needed industrial goal for, indigenous enzymes are readily unstable when subjected to harsh environmental conditions. Since the emergence of recombinant DNA technology and recent developments in protein engineering in recent years, there have been continuous reports regarding enzyme stability – most especially by the introduction of site-directed mutagenesis. With these new developments, scientists have been able to engineer enzymes using a variety of strategies in rational design such as the introduction of disulfide bridges and engineering hydrophobic residues. This review aims to highlight rational design methods and enzyme immobilization from various studies, which may be used to increase stability in industrial enzymes.
Keywords
Protein Engineering, Stability, Rational Design, Immobilization
To cite this article
Abubakar Muhammad Nazif, Ayuba Yohanna Musa, Muhammad Muawiya Alkali, Ilesanmi Esther, Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review, American Journal of Chemical Engineering. Vol. 5, No. 6, 2017, pp. 135-139. doi: 10.11648/j.ajche.20170506.13
Copyright
Copyright © 2017 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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