Promotive and inhibitory effects of raw starch adsorbable fragments from pancreatic alpha-amylase on enzymatic digestions of raw starch.
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.
Hayashida
S
S
Department of Agricultural Chemistry, Kyushu University, Fukuoka, Japan.
Teramoto
Y
Y
Kira
I
I
D000327:Adsorption; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D010179:Pancreas / Q000201:enzymology*; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D013213:Starch / Q000378:metabolism*; D013552:Swine; D014357:Trypsin; D000516:alpha-Amylases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D002241:Carbohydrates; D010446:Peptide Fragments; D013213:Starch; D000516:alpha-Amylases; D014357:Trypsin