Abstract
Amidase from Bacillus sp. APB-6 with very good acyltransferaseactivity was purified to homogeneity with a purification fold of 3.68 and 53.20% enzyme yield. The purified protein's subunitmolecular mass was determined approximately 42kDa. Hyperactivity of the enzyme was observed at pH 7.5 (150mM, potassium-phosphate buffer) and 50°C of incubation. An enhancement in activity up to 42% was recorded with ethylenediaminetetraacetic acid and dithiothreitol. The kinetic parameter K m values for substrates: acetamide and hydroxylamine-hydrochloride were 73.0 and 153mM, respectively. Further, the V max for acyltransferase activity was 1667 U/mg of protein and the K i for acetamide was calculated as 37.0mM. The enzyme showed tolerance to various organic solvents (10%, v/v) and worked well in the biphasic reaction medium. The acyltransferase activity in presence of solvents i.e. biphasic medium may prove highly favorable for the transformation of hydrophobic amides, which otherwise is not possible in simple aqueous phase.
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