Production and characterization of acyl transfer activity of amidase from Alcaligenes sp. MTCC 10674 for synthesis of hydroxamic acids

Abstract

Alcaligenes sp. MTCC 10674 has been isolated as a nitrile degrading bacterium from the soil. Amidase of this organism exhibited dual activity i.e. hydrolase as well as acyl transfer. The acyltransfer activity of this organism has been used for the synthesis of variety of hydroxamic acids. Optimization of physiochemical parameters resulted into 30 folds increase in the acyl transfer activity of amidase (0.039 Umgdcm-1 to 1.17 Umgdcm-1). The acyl transfer activity of amidase of this organism has broader substrate affinity ranging from a variety of aliphatic amides (formamide, acetamide, propanamide etc.) to aromatic amides (benzamide, mandelamide, nicotinamide etc.) along with hydroxylamine for the biotransformation of these amides into corresponding hydroxamic acid. This enzyme is quite stable at 50°C with t1/2 for 8h and at 60°C this amidase have t1/2 for 1.30 h. The acyl transfer activity of amidase of Alcaligenes sp. MTCC 10674 under high temperature condition makes of potential application in developing a bioprocess for the production of variety of aliphatic and aromatic hydroxamic acid. © 2013 Ravi Kant B, et al.