Creating and characteristics of a novel biomacromolecules complex of pea protein isolated-tannic acid-magnesium ion

Pea protein isolate (PPI) was used as a carrier matrix to load tannic acid (TA) due to its multiple cavity structures and reaction sites, after that, magnesium ion (M) was further added to form more stable carrier structures. PPI was covalently bound with TA to form TA-PPI complexes in alkaline conditions, then M induced the aggregation of TA-PPI to produce M-TA-PPI complexes. TA mainly interacted with free amino groups and sulfhydryl groups of PPI, thereby decreasing their content in complexes. TA further decreased the α-helix content and increased the β-sheet and β-turn content in TA-PPI complexes correspondingly, nevertheless the M would decline these changes in M-TA-PPI complexes. As a result of binding, TA and M jointly increased the average molecular size of complexes. The higher TA addition amount (10–20 mg/g PPI) was conducive to the stronger intramolecular interactions (more hydrophobic interactions and disulfide bonds), gel structure (higher hardness value) and storage modulus in M-TA-PPI gels. Compared with TA-PPI complexes, M-TA-PPI complexes showed higher stability in gastric digestion and higher TA releasement and antioxidant capacity of its digesta in intestinal digestion. This kind of metal-phenolics-protein complexes may have potentials to be a stable and efficient carrier for loading gastric sensitive polyphenols.