Department of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, 361021, China.
Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China.
Appl Biochem Biotechnol. 2020 Jan;190(1):18-29. doi: 10.1007/s12010-019-03091-1. Epub 2019 Jul 12.
NAD(P)H-dependent enzymes are ideal biocatalysts for the industrial production of chiral compounds, such as chiral alcohols, chiral amino acids, and chiral amines; however, efficient strategies for the regeneration of coenzyme are expected as costly of the coenzymes. Herein, a solvent-tolerant isopropanol dehydrogenase (IDH) showing lower similarity (37%) with other proteins was obtained and characterized. The enzyme exhibits high catalysis ability of its substrates methanol, ethanol, ethylene glycol, glycerol, isopropanol, n-butanol, isobutanol, and acetone. And it has good adaptability in organic solvents (isopropanol, acetonitrile, acetone, and acetophenone). Interaction force and the corresponding amino acid residues between IDH and NAD or NADP were parsed by docking. The wide substrate spectrum, excellent organic solvent tolerance, and good biocatalytic activity make the excavated enzyme a promising biocatalyst for the production of chiral compounds industrially and the construction of coenzyme regeneration systems in aqueous organic phase or organic phase.
NAD(P)H 依赖的酶是手性化合物（如手性醇、手性氨基酸和手性胺）工业生产的理想生物催化剂；然而，由于辅酶成本高昂，因此需要高效的辅酶再生策略。本文获得并表征了一种与其他蛋白质相似度较低（37%）的耐溶剂异丙醇脱氢酶（IDH）。该酶对其底物甲醇、乙醇、乙二醇、甘油、异丙醇、正丁醇、异丁醇和丙酮表现出较高的催化能力。并且它在有机溶剂（异丙醇、乙腈、丙酮和苯乙酮）中具有良好的适应性。通过对接解析了 IDH 与 NAD 或 NADP 之间的相互作用力及相应的氨基酸残基。该酶广泛的底物谱、出色的有机溶剂耐受性和良好的生物催化活性使其成为一种有前途的生物催化剂，可用于手性化合物的工业生产以及水相有机相或有机相中的辅酶再生系统的构建。
