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.
Highlights
The speed of sequencing of microbial genomes and metagenomes is providing an ever increasing resource for the identification of new robust biocatalysts with industrial applications for many different aspects of industrial biotechnology [1]
Rational design is a strategy in protein engineering where proteins with improved characteristics are created based on the available information obtained from the three- dimensional structure and the relationship between protein structure and its function, which scientists believe over the years play a crucial role in proteins function
Enzyme stability is the net balance of forces which determines whether a protein would be in its native folded conformation or a denatured state
Summary
The speed of sequencing of microbial genomes and metagenomes is providing an ever increasing resource for the identification of new robust biocatalysts with industrial applications for many different aspects of industrial biotechnology [1]. The limiting factor in the industrial application of enzymes, is the high cost of isolating and purifying large amounts that would meet industrial requirements but, beyond cost there are other limitations associated with industrial enzymes especially, the conditions subjected to industrial processes differ with that of physiological pathways, and even the desired industrial application may differ significantly from physiological roles. To overcome these limitations, tailor-made biocatalysts can be created from wild-type enzymes by protein engineering using computer-aided molecular modeling and site-directed mutagenesis (cited in [6]). Methods for maximizing stability in industrial enzymes and enzyme immobilization, concentrating on methods published in the last two decades were discussed
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