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- Title
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.
- Authors
Sun, Huihui; Gao, Wenyuan; Fan, Haiyang; Wang, Hualei; Wei, Dongzhi
- Abstract
Objective: To examine nitrilase-mediated hydrolysis of nitriles to produce optically pure α-hydroxycarboxylic acids. Results: 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 and K of GPnor51 towards o-chloromandelonitrile were 1.9 μmol min mg protein and 0.38 mM, respectively. GPnor51 also demonstrated high enantioselectivity toward mandelonitrile and other substituted mandelonitrile. Conclusion: This enzyme has a great potential for commercial production of optically pure ( R)-mandelic acid and its derivatives.
- Subjects
NITRILASES; ENZYME analysis; HYDROLYSIS; BACTERIAL genomes; MOLECULAR structure
- Publication
Biotechnology Letters, 2015, Vol 37, Issue 8, p1655
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-015-1830-4