Abstract
The acyl transfer activity of the amidase of Alcaligenes sp. MTCC 10674 has been applied to the conversion of benzamide and hydroxylamine to benzohydroxamic acid. The unique features of the acyl transfer activity of this organism include its optimal activity at 50 °C and very high substrate (100 mM benzamide) and product (90 mM benzohydroxamic acid) tolerance among the hitherto reported enzymes. The bench scale production of benzohydroxamic acid was carried out in a fed-batch reaction (final volume 1 l) by adding 50 mM benzamide and 250 mM of hydroxylamine after every 20 min for 80 min in 0.1 M potassium phosphate buffer (pH 7.0) at 50 °C, using resting cells equal to 4.0 mg dcm/ml of reaction mixture. From 1 l of reaction mixture 33 g of benzohydroxamic acid was recovered with 24.6 g l−1 h−1 productivity. The acyl transfer activity of the amidase of Alcaligenes sp. MTCC 10674 and the process developed in the present study are of industrial significance for the enzyme-mediated production of benzohydroxamic acid.
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The authors are highly grateful to the New Delhi University Grant Commission and Department of Biotechnology (DBT) Ministry of Science and Technology New Delhi, India for providing financial assistance in the form of Junior Research Fellowship to Mr. Ravi Kant Bhatia and Senior Research Fellowship to Mr. Shashi Kant Bhatia and Mr. Praveen Kumar Mehta. The use of the computational facility at the Sub-Distributed Information Centre (SDIC), Himachal Pradesh University, Shimla is also duly acknowledged.
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Bhatia, R.K., Bhatia, S.K., Mehta, P.K. et al. Bench scale production of benzohydroxamic acid using acyl transfer activity of amidase from Alcaligenes sp. MTCC 10674. J Ind Microbiol Biotechnol 40, 21–27 (2013). https://doi.org/10.1007/s10295-012-1206-x
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DOI: https://doi.org/10.1007/s10295-012-1206-x