Mechanism of peptides from rice hydrolyzed proteins hindering starch digestion subjected to hydrothermal treatment.

Clarifying the interactions between food components is critical in designing carbohydrate-based foods with low digestibility. To date, the hindering effect of starch-protein interactions on starch digestion has attracted extensive attention. In this study, rice proteins were further hydrolyzed, and rice peptides (RP) with different molecular weights were obtained by ultrafiltration. The effects and possible mechanisms of RP with different molecular weights on the structure, thermal properties, and in vitro digestibility of cooked rice starch were investigated. All peptides slowed the digestion of rice starch in a concentration-dependent manner. A concentration of 10% RP >10 decreased the rapidly digestible starch content from 68.02 to 45.90 g/100 g, and increased the resistant starch content from 17.54 to 36.54 g/100 g. The addition of RP improved the thermal stability of the starch and reduced the amount of leached amylose. Infrared analysis shows that strong hydrogen bonds formed between RP (especially RP >10 ) and starch during co-gelatinization. In addition, RP improved the compactness of aggregated structure and played an important role in hindering the enzymatic hydrolysis of starch. These results enrich the theory of starch-protein interactions and have important implications for the development of carbohydrate-based foods with low digestibility and protein functional foods.