Characterization of Amylase Inhibitor from the Seeds of Mucuna utilis

Proteinaceous amylase inhibitors are present in plants which regulate the activity of amylases. An αAmylase inhibitor was isolated and purified by conventional protein purification techniques (ammonium sulphate fractionation, Sephadex G-10, sephadex G-50 chromatography and HPLC) from Mucuna utilis seeds. Its molecular weight as determined by gel-permeation chromatography on Sephadex G-100 was found to be 15 kDa. The purified inhibitor was temperature stable and retained more than 75% activity at 65 °C. Inhibitor was found to have pH optima of 6.9. 100% Zone of inhibition was observed when the inhibitor was added on the plated organisms. The Mucuna utilis amylase inhibitor was found to inhibit the activity of human salivary αamylase. Inhibitory activity of α-amylase inhibitor against mammalian amylases could suggest its potential in treatment of diabetes and cure of nutritional problems, which result in obesity.