EXTRACTION, PURIFICATION AND SOME PARTIAL CHARACTERIZATION OF ALPHA-AMYLASE INHIBITORS FROM WHEAT LAPAR 28-IGAPO

alpha-Amylase inhibitors from wheat (Triticum aestivum) cultivar lapar 28-Igapo were extracted with water in a 1:10 (w:v) ratio and precipit ated with ammonium sulfate between 20-50% saturation, followed by DEAE and CM-cellulose chromatography. One inhibitor was purified and desig nated as CMC-IB, and had electrophoretic mobilities of 0.23 and 0.54 i n alkaline and acidic conditions, respectively. This inhibitor was 750 times more active on human salivary alpha-amylase (HSSA) than porcine pancreatic sigma-amylase (PPA). The preincubation time required for m aximum complexation with HSA was 20 minutes and optimum pH of inhibiti on was 7.5. The inhibitor CMC-IB was stable at 0 degrees C and maintai ned 50% of inhibitory activity against HSA, when incubated at 98 degre es C for one hour.