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dc:title "HTML Summary of #2945 \n\nBiotransformations Using Nitrile Hydrolysing Enzymes For
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bibo:abstract "Nitrile hydrolysing enzymes have found wide use in the pharmaceutical industry for the\nproduction of fine chemicals. This work presents a strategy that facilitates the rapid\nidentification of bacterial isolates demonstrating nitrile hydrolysing activity. The\nstrategy incorporates toxicity, starvation and induction studies along with subsequent\ncolorimetric screening for activity, further focusing the assessment towards the\nsubstrates of interest. This high-throughput strategy uses a 96 well plate system, and has\nenabled the rapid biocatalytic screening of 256 novel bacterial isolates towards β-\nhydroxynitriles. Results demonstrate the strategy’s potential to rapidly assess a variety\nof β-hydroxynitriles including aliphatic, aromatic and dinitriles. A whole cell catalyst\nRhodococcus erythropolis SET1 was identified and found to catalyse the hydrolysis of\n3-hydroxybutyronitrile with remarkably high enantioselectivity under mild conditions,\nto afford (S)-3-hydroxybutyric acid in 42% yield and >99.9% ee. The biocatalytic\ncapability of this strain including the variation of parameters such as temperature and\ntime were further investigated and all results indicate the presence of a highly\nenantioselective if not enantiospecific nitrilase enzyme within the microbial whole cell.\nWe present substrate evaluation with 34 chiral nitriles of Rhodococcus erythropolis\nSET1. These substrates consist primarily of β-hydroxy nitriles with varying alkyl and\naryl groups at the β-position containing in some cases, various substituents at the α-\nposition. In the case of β-hydroxy nitriles unsubstituted at the α-position, acids were the\nmajor products as a result of suspected nitrilase activity of the isolate. Unexpectedly,\namides were found to be the major products when β-hydroxynitriles were substituted at\nthe α-position with a vinyl group. Therefore this novel isolate has demonstrated\nadditional NHase behaviour which is dependent on the functionality at the α-position. In\norder to probe this mechanism further related substrates were evaluated and amide was\nobserved where other electron withdrawing groups were present at the α-position.\nAdditionally various parameters which may influence the biocatalytic hydrolysis by\nSET1 were studied and are presented herein."^^xsd:string;
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foaf:givenName "Tracey"^^xsd:string;
foaf:name "Tracey Coady"^^xsd:string;
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