Abstract
The enzymatically inactive but raw-starch-adsorbable peptide fragments designated as Gp-pan P and Gp-pan I were obtained from a tryptic digest of heat-inactivated hog pancreatic alpha-amylase. These two glycopeptide fragments were purified with Sephadex G-75, DEAE-Sephadex A-50, and HPLC and were found to be homogeneous on disc gel electrophoresis. Gp-pan P and I had molecular weights of 20,000 and 30,000 with SDS-PAGE, carbohydrate contents of 10% and 7%, N-terminal amino acids Gly-Trp and Ala-Val, and C-terminal amino acids Gly-Arg and Ile-Lys. Gp-pan P had promotive but Gp-pan I inhibitory effects on raw starch digestion by Aspergillus awamori var. kawachi glucoamylase I and Bacillus subtilis 65 alpha-amylase.
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