Abstract: To investigate the inhibitory mechanism of small peptides on carbohydrate digestion, α-amylase and α-glucosidase inhibitory fractions from the water extract and the gastropancreatic digest of dry-cured ham muscle of Wanzhe spotted pigs were separated, purified, identified, and screened for peptide sequences. And the quantum chemical calculation was used to calculate structural and charge parameters including the distribution and energy of the frontier orbitals, electrostatic charge distribution and bond length, in order to speculate the active sites. It was found that the particle size of ham muscle decreased and its hypoglycemic activity increased after proteolysis. Two (S-I and S-II) and three fractions (WY-I, WY-II and WY-III) were obtained from the water extract and the digest after Sephadex column chromatography, respectively. Using mass spectrometry, 104 peptide sequences consisting of 8–24 amino acids were identified from fraction WY-II and five sequences with Peptide Ranker scores greater than 0.7 were selected. The highest occupied orbitals of the five sequences were mainly distributed in the guanidine groups of arginine and the groups close to the amino-terminal end, while the lowest unoccupied orbitals were in the carboxyl terminals and nearby groups. Sequences with lower ΔEL-H values, GPMGPSGPR, LGFGGPSGPNAGR and APAPAPAPAPPK, might be more active. According to Coulomb’s law, the active sites of these three peptides were located at –C106H108 of arginine, –C10H12 of leucine and –C176H177 of lysine, respectively. This study could provide theoretical support for understanding the blood glucose-regulating mechanism of peptides and the nutritional value of local pig breeds.

Key words: hypoglycemic; α-amylase and α-glucosidase inhibitory activities; peptide sequences; quantum chemical calculation; dry-cured ham