化学
酯酶
吲哚
羧酸盐
突变体
酶
大肠杆菌
分辨率(逻辑)
立体化学
羧酸
有机化学
生物化学
基因
计算机科学
人工智能
作者
Hongjun Zhang,Zeguang Cheng,Litian Wei,Xinjun Yu,Zhao Wang,Yinjun Zhang
标识
DOI:10.1016/j.bioorg.2022.105602
摘要
A gene encoding an esterase from Bacillus aryabhattai (BaCE) was identified, synthesized and efficiently expressed in the Escherichia coli system. A semi-rational protein engineering was applied to further improve the enzyme's enantioselectivity. Under the guidance of the molecular docking result, a single mutant BaCE-L86Q and a double mutant BaCE-L86Q/G284E were obtained, with its Emax value 6.4 times and 13.9 times of the wild-type BaCE, respectively. The recombinant BaCEs were purified and characterized. The overwhelming E value demonstrated that BaCE-L86Q/G284E was a promising biocatalyst for the biological resolution to prepare (S)-indoline-2-carboxylic acid.
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