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• W2025145428 abstract "Arylacetonitrilases from Aspergillus niger CBS 513.88 and Neurospora crassa OR74A (NitAn and NicNc, respectively) were expressed in recombinant Escherichia coli JM109. The respective whole-cell catalysts preferentially hydrolyzed (R)-enantiomers of (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile. NitNc also formed significant amounts of mandelamide from (R,S)-mandelonitrile (40% of total product), mainly found as the (S)-enantiomer. At pH 4.5 and 5.0, the cells retained more than 40 and 60% of their nitrilase activity at pH 7, respectively. Nitrilase variants generated by site-directed mutagenesis carried amino acid replacements in the vicinity of the catalytically active cysteine residues (C162 and C167 in NitAn and NitNc, respectively). The conversions of (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile by the nitrilase variants were compared to the wild-type nitrilases in terms of activity, enantioselectivity, and acid/amide ratio of the products formed. Thus the W168A variant of NitNc was identified, which formed significantly increased amounts of mandelamide and 2-phenylpropionamide, and which demonstrated an almost complete inversion of enantioselectivity for the conversion of (R,S)-2-phenylpropionitrile (from R- to S-selectivity)." @default.
• W2025145428 created "2016-06-24" @default.
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• W2025145428 date "2012-05-01" @default.
• W2025145428 modified "2023-10-17" @default.
• W2025145428 title "Influence of point mutations near the active site on the catalytic properties of fungal arylacetonitrilases from Aspergillus niger and Neurospora crassa" @default.
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• W2025145428 doi "https://doi.org/10.1016/j.molcatb.2012.01.005" @default.
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