PURIFICATION AND CHARACTERIZATION OF AN ?-AMYLASE INHIBITOR FROM MAISE (ZEA MAIZE)

Publisher Website
Google Scholar
Abstract
α-Amylase inhibitor is presented in maize seeds. It is a protein as indicated by precipitation with ammonium sulfate and trichloroacetic acid, denaturation by heat, digestion with proteases and by dye-staining. It was purified to homogeneity by ammonium sulfate precipitation and Sephadex G-75 gel filtration. It had an apparent molecular weight of 29,600 and did not contain any carbohydrate. Its properties differed from those of previously reported α-amylase inhibitors, since it was active against α-amylase of maize, produced during germination as well as against Bacillus subtilis α-amylase. It was also active against α-amylase from the insects Tribolium castaneum, Sitophilus zeamais and Rhyzopertha dominica, but it was inactive against α-amylase from human saliva, hog pancreas, Aspergillus oryzae, wheat, rye, barley, triticale, and sorghum. It was stable for 5 min at 96°C at pH 7. Maximal inhibition required at least 10 min of preincubation with the enzyme at pH 6.8 and 257deg;C. Polyacrylamide gel electrophoresis gave three protein bands, but only one was obtained in S.D.S. and mercaptoethanol.