文献类型：期刊文献

英文题名：Cloning, purification and evaluation of the enzymatic properties of a novel arylacetonitrilase from Luminiphilus syltensis NOR5-1B: a potential biocatalyst for the synthesis of mandelic acid and its derivatives

作者：Sun, Huihui[1];Gao, Wenyuan[1];Fan, Haiyang[1];Wang, Hualei[1];Wei, Dongzhi[1]

机构：[1]E China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2015

卷号：37

期号：8

起止页码：1655

外文期刊名：BIOTECHNOLOGY LETTERS

收录：;EI(收录号：20151600749318);WOS:【SCI-EXPANDED(收录号:WOS:000357034800016)】；

基金：This work was supported by the National Natural Science Foundation of China (No. 21406068/B060804) and China Postdoctoral Science Foundation funded Project (No. 2014M560308) and National major science and technology projects of China (2012ZX09304009).

语种：英文

外文关键词：Arylacetonitrilase; (R)-o-Chloromandelic acid; Luminiphilus syltensis; Mandelonitrile derivatives; Nitrilase

摘要：To examine nitrilase-mediated hydrolysis of nitriles to produce optically pure alpha-hydroxycarboxylic acids. A novel nitrilase, GPnor51, from Luminiphilus syltensis NOR5-1B was discovered by genomic data mining. It could hydrolyze racemic o-chloromandelonitrile to (R)-o-chloromandelic acid with high enantioselectivity (ee 98.2 %). GPnor51 was overexpressed in Escherichia coli BL21 (DE3), purified, and its catalytic properties studied. GPnor51 had a broad substrate acceptance toward various nitriles with structure diversity. It was an arylacetonitrilase that uses arylacetonitriles as optimal substrates. The V (max) and K (m) of GPnor51 towards o-chloromandelonitrile were 1.9 mu mol min(-1) mg(-1) protein and 0.38 mM, respectively. GPnor51 also demonstrated high enantioselectivity toward mandelonitrile and other substituted mandelonitrile. This enzyme has a great potential for commercial production of optically pure (R)-mandelic acid and its derivatives.