Abstract
Enzymes from extremophiles are creating interest among researchers due to their unique properties and the enormous power of catalysis at extreme conditions. Since community demands are getting more intensified, therefore, researchers are applying various approaches viz. metagenomics to increase the database of extremophilic species. Furthermore, the innovations are being made in the naturally occurring enzymes utilizing various tools of recombinant DNA technology and protein engineering, which allows redesigning of the enzymes for its better fitment into the process. In this review, we discuss the biochemical constraints of psychrophiles during survival at the lower temperature. We summarize the current knowledge about the sources of such enzymes and their in vitro modification through mutagenesis to explore their biotechnological potential. Finally, we recap the microbial cell surface display to enhance the efficiency of the process in cost effective way.
Highlights
As proven through research, living creatures are omnipresent, leaving no space vacant ranging from hydrothermal vents to glaciers
For improving the existing enzymes, there are two approaches that allow redesigning of the enzyme, which may either enhance the activity or limit the inhibitory challenges of the enzyme (1) Rational redesign- as the name suggests it redesigns the existing biocatalyst using site-directed mutagenesis, requiring full knowledge of 3-D protein structures and the mechanism of enzymatic reaction (2) Random mutagenesis method such as directed evolution, it mimics the natural process of variant generation and includes all molecular techniques for variant generation such as repeated oligonucleotide directed mutagenesis, error prone PCR, and chemical agents
One variant (32G7) of subtilisin S41 was created by random mutagenesis, saturation mutagenesis, and in vitro recombination/DNA shuffling, a remarkable improvement in temperature range was observed without compromise in its catalysis at low temperatures, and developed threefold higher catalytic efficiency (Lillford and Holt, 2002)
Summary
As proven through research, living creatures are omnipresent, leaving no space vacant ranging from hydrothermal vents to glaciers. Some species have adapted themselves to an extreme environment, by acquiring range of adaptations for survival, at each level of cell function and structure (Feller, 2013) This unique attribute has created keen interest among the researchers to resolve the mystery of such living organisms. The cold-active enzymes provide the liberty to conduct the chemical reaction at fairly good reaction rate at low temperatures. The reason behind their enhanced catalysis at low temperature is because of the optimization of their electrostatics at or nearby active site. Current Technological Improvements in Enzymes the goal reaction These atypical properties place the coldactive enzymes on top in industrial demand list, as the market competes for cost effectiveness and quality product. We describe these two approaches to obtain useful and applicable enzymes
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