Characterization of α-Amylase Binding Agents from Hawthorn Leaf Using Ultrafiltration and Liquid Chromatography Tandem Mass Spectrometry

An affinity based ultrafiltration method was established to rapid screening amylase inhibitors from hawthorn leaf. Various factors were optimised including the pH of the incubation buffer, ion strength, incubation time, incubation temperature and the concentration of a-amylase. Kaemp-ferol was chosen as a model compound. The condition chosen for screening was as follows: pH 7.4, ion strength 10 mmol/L, incubation time 45 min, incubation temperature 37 degrees C, amylase concentration 10 g/L. Then, the established method was applied to screening alpha-amylase inhibitors from extract of hawthorn leaf and three active compounds were obtained.