Comparison and inhibition mechanism study on the in vitro digestibility of rice starch complex with soy β-conglycinin and soy glycinin

• Published in: Food hydrocolloids Vol. 154; p. 110071
• Main Authors: Shi, Xin, Li, Xuxu, Wang, Ruifeng, Niu, Meng, Zhao, Siming
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.09.2024
• Subjects: Aggregated structure; In vitro digestion; Interaction forces; Physical barrier; Rice starch; In vitro digestion; Rice starch; Physical barrier; Interaction forces; Aggregated structure
• ISSN: 0268-005X; 1873-7137
• DOI: 10.1016/j.foodhyd.2024.110071

To inhibit the digestion of indica rice starch (IRS), an excellent strategy was to add exogenous proteins that interact with IRS, which was closely associated with the protein components. Herein, this study compared the effects of soy protein subfractions, soy β-conglycinin (7S) and soy glycinin (11S), on IRS digestion and explored its inhibition mechanisms. This study used hydrothermal processing to prepare IRS complexes with soy protein subfractions (7S and 11S) at different starch-protein ratios. The results found that adding 7S and 11S exhibited different inhibitory patterns on starch digestion. Compared to IRS, a higher slowly digestible starch (SDS) content (40.91%, p < 0.05) was observed at the IRS-7S ratios of 20:8, while the 20:6 IRS-11S complex showed a higher resistant starch (RS) content (15.76%, p < 0.05). Subsequently, the interactions between IRS and soy protein subfractions and their multi-scale structural changes were explored. The rheological results revealed that hydrophobic interaction and hydrogen bonding were the main driving forces. Various structural changes were closely associated with inhibitory modes of soy protein subfractions on IRS digestion. In detail, the increased SDS content in IRS-7S complexes was attributed to the formation of compact protein physical barriers, aggregated structures with more ordered regions, and flexible secondary conformations of 7S. However, the high-density structures and the stable secondary conformations of 11S were responsible for the increased RS content in IRS-11S complexes. Thus, this study could provide directions for developing SDS-enriched or RS-enriched starch-based products. [Display omitted] •Adding 7S and 11S exhibited different inhibitory modes on starch digestion.•Hydrophobic interaction and hydrogen bonding were the main driving forces.•The compact protein barrier played a key role in the increased SDS of IRS-7S complex.•The high-density structure was responsible for the increased RS in IRS-11S complex.