Design and Evolution of Biocatalysts

Abstract

Enzymes as biocatalysts offer several advantages over their chemical counterparts, and as such have attracted much attention for use in the synthesis of various organic compounds. However, despite many successes in the practical application of enzymes, the extensive use of enzymes in the synthesis of organic compounds is still hindered by inadequacy in substrate specificity, catalytic activity, enantio-selectivity and stability. Enzymes with desired functions targeted for practical applications have long been a goal in protein/enzyme engineering. Many approaches have been developed and employed for redesigning enzymes with desired properties, including the structure-guided rational method, directed evolution, computational methods, and combinatorial methods. This review will cover recent advances in the design and evolution of enzymes targeted for specific properties, focusing on the strategy and the applicability of each approach.

Validating computer simulations of enantioselective catalysis; reproducing the large steric and entropic contributions in Candida Antarctica lipase B

“…Optimizing enzymes to catalyze selective enantioselective reactions has a major potential in biotechnology, including in the generation of biocatalysts for efficient synthesis of enantiomerically pure chiral molecules for the production of drugs by the pharmaceutical industry …”

“…Recent advances in this field have been due, in part, to directed evolution experiments with some qualitative insight from theoretical studies (see Introduction). However, it seems to us that at the present stage it is important to push the capacity of theoretical simulation as useful tool in designing enantioselective enzymes.…”