Rhodococcus rhodochrous PA-34 has been reported to produce nitrile hydratase enzyme that converts 3-cyanopyridine to nicotinamide. A mutant of R. rhodochrous PA-34 was generated through chemical mutagenesis using N-methyl-N-nitro-N-nitrosoguanidine (MNNG) that exhibited 2 times higher nitrile hydratase activity as compared to wild strain. The reaction conditions using resting cells of this mutant strain for the conversion of nicotinamide were optimized. Under the optimized reaction conditions the mutant strain exhibited maximum nitrile hydratase activity [7.8 U/mgdcm (milligram dry cell mass)] at 55 degrees C in 0.3 M potassium phosphate buffer (pH 5.5).
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Article Synopsis
- This study focuses on improving the enzyme Fe-type Nitrile hydratase (Fe-type NHase) from Pseudomonas fluorescens by mutating a specific residue (Q86) in its substrate access tunnel, which enhanced its catalytic performance.
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- Structural analyses revealed changes in the enzyme's entrance tunnel and substrate-binding pocket, which contributed to a shift in substrate preference from aliphatic to aromatic nitriles, supported by molecular dynamics simulations.
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