Purification and Characterization of Amylase Inhibitors from the Seeds of Senna Alata
Journal Title: IOSR Journal of Pharmacy (IOSRPHR) - Year 2018, Vol 8, Issue 4
Abstract
An α-Amylase inhibitor was isolated and purified employing ammonium sulphate fractionation, Sephadex G-10, sephadex G-50 chromatography and HPLC from the seeds of Senna alata. The molecular weight determined by SDS – PAGE and Sephadex G-100 chromatography was found to be 10 – 11 kDa. The inhibitor was retained 40% and 65% at pH 2.0 and 10.0 respectively, indicated its stability in a broad pH range. The purified inhibitor was stable in a temperature range from 4˚C to 65˚C. Purified inhibitor also inhibited the human salivary amylase which suggests that the amylase inhibitor of Senna alata can be used to treat nutrition related problems.
Authors and Affiliations
K S Chandrashekharaiah
Keywords
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