Efficient and easible biocatalysts: Strategies for enzyme improvement. A review

Owing to the environmental friendliness and vast advantages that enzymes offer in the biotechnology and industry fields, biocatalysts are a prolific investigation field. However, the low catalytic activity, stability, and specific selectivity of the enzyme limit the range of the reaction enzymes involved in. A comprehensive understanding of the protein structure and dynamics in terms of molecular details enables us to tackle these limitations effectively and enhance the catalytic activity by enzyme engineering or modifying the supports and solvents. Along with different strategies including computational, enzyme engineering based on DNA recombination, enzyme immobilization, additives, chemical modification, and physicochemical modification approaches can be promising for the wide spread of industrial enzyme usage. This is attributed to the successful application of biocatalysts in industrial and synthetic processes requires a system that exhibits stability, activity, and reusability in a continuous flow process, thereby reducing the production cost. The main goal of this review is to display relevant approaches for improving enzyme characteristics to overcome their industrial application. [Display omitted] •Computational Methods enable extensive in silico screening of redesigned enzyme variants, curtailing experimental processes.•Targeted mutagenesis methods (SSM and CAST), pinpoint specific structural regions.•Cross-linking and ionic bonding are effective approaches enhancing enzyme properties for industrial processes.•Cross-linking with glutaraldehyde and PEGylation enhances enzyme resilience to denaturation and improve solubility.•Integration of physicochemical, chemical, and immobilization techniques, enhances enzyme performance economically.