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Title of Journal: Biotechnol Lett

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Abbravation: Biotechnology Letters

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Springer Netherlands

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DOI

10.1016/j.ast.2014.05.009

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1573-6776

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Expression characterization of a novel nitrilase

Authors: Huihui Sun Wenyuan Gao Hualei Wang Dongzhi Wei
Publish Date: 2015/11/12
Volume: 38, Issue: 3, Pages: 455-461
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Abstract

A novel nitrilase PpL19 from Pseudomonas psychrotolerans L19 was discovered by genome mining It showed Sselectivity with an enantiomeric excess of 527  when used to hydrolyse R Smandelonitrile No byproduct was observed PpL19 was overexpressed in Escherichia coli BL21 DE3 and formed inclusion bodies that were active toward mandelonitrile and stable across a broad range of temperature and pH In addition PpL19 hydrolysed nitriles with diverse structures arylacetonitriles were the optimal substrates Homology modelling and docking studies of both enantiomers of mandelonitrile in the active site of nitrilase PpL19 shed light on the enantioselectivity

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