Fabrication of tannins and oat protein non-covalent complexes: Effect on the structure and in vitro digestion properties of oat proteins.

This study explored the non-covalent interactions between oat protein isolate (OPI) and two tannic compounds-proanthocyanidins (PA) and tannic acid (TA)-and examined their impact on the structural and digestive properties of oat proteins. The combination of OPI with tannic compounds formed granular complexes with particle sizes ranging from 126 to 240 nm and zeta potentials between -35 and -44 mV. Compared to OPI alone, the α-helix and β-turn contents decreased, while the β-sheet and random coil contents increased in both OPI-tannin complexes. Fluorescence spectra analysis indicated that hydrogen bonding was the main interaction force in OPI-PA complexes, while OPI and TA were primarily bound by hydrophobic interactions. The simulated digestion analysis showed that the protein digestibility was delayed in the OPI-tannin complexes, likely due to the inhibition of digestive enzyme activity by tannic compounds, which slowed OPI digestibility. Additionally, the oxidation resistance of the OPI-tannin complexes significantly improved after in vitro digestion, indicating that the non-covalent complexes provided superior protection for the tannic compounds. These findings offer theoretical support for the design and utilization of oat- and tannin-rich foods.