Abstract
Abstract Acyl transfer activity of amidase of Pseudomonas putida BR-1 has been explored for the conversion of N-substituted aromatic amide (nicotinamide) and hydroxylamine to nicotinyl hydroxamic acid. Nicotinyl hydroxamic acid is an important pharmaceutical compound with enormous biomedical applications. P. putida BR-1 produces maximum amidase acyl transfer activity 138 U/mg dcm at 50 °C, with highest conversion (95%) of nicotinamide to nicotinyl hydroxamic acid. A bioprocess was developed for production of nicotinyl hydroxamic acid in batch reaction (final volume 1 L) by adding 200 mM nicotinamide and 1000 mM of hydroxylamine in 100 mM sodium phosphate buffer (pH 7.5) at 50 °C, using 20 U/ml acyl transfer activity resting cells of P. putida BR-1 in reaction mixture. From 1 L reaction mixture 16 g of nicotinyl hydroxamic acid was recovered with 32 g/L/h volumetric productivity. The amidase acyl transfer activity of P. putida BR-1 and the process developed in the present study are of industrial significance for the enzyme mediated production of nicotinyl hydroxamic acid.
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