Enhancing thermostability of the biocatalysts beyond their natural function via protein engineering

Abstract

Majority of the naturally occurring enzymes lacks essential features required during the harsh conditions of the industrial processes, because of their less stability. Protein engineering tool offers excellent opportunity to improve the biochemical properties of these biocatalysts. These techniques further help in understanding the structure and function of the proteins. Most common methods employed in protein engineering are directed evolution and rational mutagenesis. Several research groups have utilized these methods for engineering the stability/activity of diverse class of enzymes. In silico tools further plays an important role in designing better experimental strategy to engineer these proteins. The availability of vast majority of data on protein thermostability will enable one to envisage the possible factors that may contribute significantly in maintaining the protein structure and function during various physical conditions. This review discusses the common method employed in protein engineering along with various molecular/computational approaches that are being utilized for altering protein activity, along with important factors associated with these processes.