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An a-Amylase inhibitor was isolated and purified employing ammonium sulphate fractionation, molecular sieve chromatography on sephadex G-10 and G-50 and HPLC from the seeds of Adenanthera pavonina. The molecular weight was found to be 10 12 kDa as determined by gel-permeation chromatography on Sephadex G-100. The specific inhibitor activity, fold purity and the yield obtained for Adenanthera pavonina amylase inhibitor was 32.12, 51 and 13.07, respectively. The purified inhibitor was heat stable and retained more than 52% activity at 65 °C. The optimum pH obtained for purified inhibitor was 6.3 and 100% Zone of inhibition was observed when it was added on the plated organisms. The Adenanthera pavonina amylase inhibitor inhibited the activity of human salivary a-amylase and inhibitory activity of a-amylase inhibitor against mammalian amylases could suggest its potential in treatment of diabetes and related nutritional problems results in obesity.

Studies on the Amylase Inhibitors from the Seeds of Adenanthera Pavonina