Design and Evolution of Biocatalysts

Sang-Chul      Lee; Jin-Hyun      Kim; Hak-Sung      Kim

doi:10.2174/138527210792927609

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.

Keywords: Biocatalyst, rational design, directed evolution and computational design, computational, stability, catalytic efficiency, enantioselectivity, 3-D structure, error-prone PCR, DNA shuffling, loop remod-eling, in silico mutagenesis, multiple saturation mutagenesis, CAST, chiral compounds, immobilization, Xylanase A, pH 9.0 agar plate, Mandelamide hydrolase, Pseudomonas putida, CtXR, MAO-N, PheDH, L-phenylalanine, hGDA, D-hydantoinase, (D-HPH), Exo-chitosanase, Bbchit1, CGTase, FACS, GlyII, MBL, SIAFE, (BVMO), PFE, NADH, NADPH, SCR, kcat/KM