IMMOBILIZATION AND REACTION CONDITION OPTIMIZATION OF AMIDASE OF BACILLUS SP. MNB-1

Abstract

Amidase is a nitrile metabolizing enzyme, belongs to the family of hydrolases, which acts on carbon-nitrogen bonds other than peptide bonds. It catalyzes hydrolysis of amide to carboxylic acid and ammonium. Amidases find wide applications in various industries as commodity chemicals (e.g. acrylic acid, nicotinic acid etc ).or pharmaceutically important acids (organic acids and hydroxamic acids). Characterization of bacterial strain was carried out and expected to be Bacillus subtilis. The bacterial cells, which produce amidase enzyme, were immobilized in sodium aliginate and agarose with agar polymer gels. The optimum pH, temperature and substrate specificity, substrate concentration, metal ion effect, reusability and cell viability for the activity of amidase in the immobilized cells were analyzed, respectively. The enzyme activity of the immobilized cells shows optimum activity with in a wide range of pH (6-9) temperature (20-40oC) and substrate concentration (30mM-70mM). The reusability and cell viability also increased considerably. The amidase of the immobilized cells was reported slightly more stable and active in calcium alginate matrix than agarose+agar matrix however, both the candidate are efficient to be used in production of important products at bioreactor level.