Contrasting structural evolution of starch and protein in aged wheat is associated with interfacial disintegration: implications for nutrient utilization and predictive modeling

Multiscale structural remodeling of highland barley starch by Monascus fermentation: Chain-length redistribution drives V-type ordering and enhances resistant starch.

Monascus fermentation is a food-compatible strategy for regulating starch digestibility, but the multiscale structural basis of resistant starch (RS) formation remains insufficiently understood. In this study, highland barley starch (HBS) was fermented for 6, 8, 10, and 12 days to clarify the depolymerization-rearrangement-V-type ordering pathway. Fermentation markedly reduced molecular size, with Mw/Mn decreasing from approximately 76/17 × 106 g/mol in HBS to 14/3 × 106 g/mol at day 8 and 3/0.7 × 106 g/mol at day 12. FBS-8 showed the greatest enrichment of DP 100-5000 chains and the strongest A-to-V structural transition, accompanied by the highest RS content (60.41%) and the lowest predicted glycemic index (pGI). FTIR and DSC results further indicated hydrogen-bond reorganization and the formation of thermally stable ordered domains, whereas prolonged fermentation partly disrupted the optimal precursor pool. These findings identify 8 days as the optimal fermentation period under the present conditions and provide a structural basis for developing high-RS cereal starch ingredients with potentially lower predicted glycemic impact.

Study on the mechanism of starch granule-associated proteins in fermented barley on starch digestibility.

This study aimed to elucidate how fermentation regulates the composition of starch granule-associated proteins (SGAPs) and starch granule channel proteins (SGCPs), and their relationship with starch digestibility. Qualitative proteomic analysis revealed differences in the detectable protein profiles, with F2E8J4 and P07596 detected only in F-SGAPs under the present analytical conditions. Mechanistic studies using fluorescein-labeled enzyme technology, interaction force analysis, and enzymatic reaction kinetics revealed that SGAPs impede starch-enzyme binding. Although fermentation weakened electrostatic interactions between SGAPs and starch, it optimized starch ordered structure and increased the apparent inhibitory effect on α-amylase, thereby increasing the resistance of starch to digestion. These findings indicate that fermentation reduces starch digestibility by modifying protein composition and optimizing starch structure.

STMP Crosslinking of Pigmented Whole Bao Rice Flours: Effects on Structural, Rheological, Digestive, Bioactive and Gel-Forming Properties

Mechanistic insights into structural remodeling and functional enhancement of peanut protein induced by high-speed shear processing

Methodological approaches to assess protein digestibility with an emphasis on plant-derived foods.

Ultrasound-induced modulation of structural organization and in vitro digestibility in highland barley starch-ferulic acid complexes.

This study aimed to investigate the effects of complexes formed by ultrasonicated highland barley starch (UHS) and ferulic acid (FA) at concentrations of 1% to 5% on the functional properties and digestive characteristics of starch. The XRD results showed that UHS formed more V-shaped crystal structures with FA, and the maximum amount of FA increased from 3% to 5%. Fourier transform infrared spectroscopy demonstrated that it enhanced the crystallization and hydrogen bond interaction of UHS with FA. The 1H NMR spectrum of the complex revealed a more pronounced low-field shift, confirming that ultrasonic treatment significantly enhanced the interaction between starch and FA. This results in higher crystallinity, more complex structural density, and superior viscoelastic and thermal properties, enhancing anti-digestibility and increasing anti-starch content from 20.69% to 28.22%. UT effectively modulates the complex's physicochemical and digestive properties, suggesting potential applications in functional highland food development.