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Published on 4 August 2016

Nitrilases catalyze the hydrolsis of "nitrile" derivatives into the corresponding carboxylic acids. They are present in various pathways for the biosynthesis of natural products. The LCOB (lien vers labo AZ)  wishes to study the activity and enantioselectivity of new nitrilases on a panel of cyano-alkyls.

Nitriles are important intermediates in synthetic chemistry because they are easy to prepare by addition or substitution reactions and they give access to a wide variety of carboxilic acids. However, their chemical hydrolysis requieres harsch experimental conditions and sensitive functions may be damaged. Nitrilases catalyze the hydrolysis of nitrile derivatives into the corresponding carboxylic acids. 

In contrast with the chemical hydrolysis conditions, the biocatalytic ones are mild and therefore using the biocatalysts may be a good alternative to the chemical pathway.

A high-throughput screening of candidate nitrilases against 25 structurally diverse substrates allowed us to create a wide collection of 125 experimentally validated nitrilases. The enzymes were selected by genomic approach from 700 diverse prokaryotic species and one metagenome as representative of the nitrilase family diversity. The enzymatic screening of this collection expands the biocatalytic toolbox for chemical synthesis by providing a large number of tested nitrilases with their assigned substrates​