4.5 Review

Tailoring Multipurpose Biocatalysts via Protein Engineering Approaches: A Review

期刊

CATALYSIS LETTERS
卷 149, 期 8, 页码 2204-2217

出版社

SPRINGER
DOI: 10.1007/s10562-019-02821-8

关键词

Enzyme immobilization; Biocatalysis; Protein engineering; Cross-linked enzyme aggregates; Support materials; Computational modeling

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The current industrial revolution signifies the high-value of protein engineering. The development of multipurpose biocatalysts is significantly expanding as a result of increased access and enzyme tailoring ability to satisfy the ever-increasing industrial demands. Enzyme-catalyzed processes offers multi-benefits at a time, e.g., low catalyst loading, high specificity, selectivity, mild processing for a complex and chemically unstable compounds, capability to reduce or eliminate reaction by-products, overall reusability and cost-effective ratio via immobilization, and potential to carry out conventional multi-stage processes via one-pot reaction. In this review, we critically elaborated recent achievements in applying new and/or state-of-the-art sophisticated protein engineering approaches to tailor the catalytic properties of enzymes or design enzymes with new and improved activities to catalyze desired biochemical transformations by orders of magnitude. We focused on different protein engineering approaches such as substrate engineering, medium engineering, and post-translational enzyme modification, structure-assisted protein tailoring, advanced computational modeling, and the exploration of inimitable synthetic scaffolds to develop multipurpose biocatalyst and improve the performance of multi-enzyme systems. In short, this study demonstrates an array of molecular biology insights and computational designs speeding up the tailored design of new and industrial biocatalysts. Continuous key developments in this direction together with protein engineering in unique ways might offer the ever-increasing opportunities for impending biocatalysis research for industrial bioprocesses. [GRAPHICS] .

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