Establishing a novel ternary complex of soybean protein isolated-tannic acid-magnesium ion and its properties.

A ternary complex composed of soybean protein isolated (SPI), tannic acid (TA) and magnesium ion (M) was established to enhance the capability of protein carriers for TA delivery. SPI was firstly covalently bind with TA (TA-SPI) and then M was employed to form the ternary complex (M-TA-SPI). Their structures, gel and digestion properties were further investigated. TA was observed to covalently bind with SPI. TA-SPI and M-TA-SPI complexes showed different molecule size and spatial structures after binding with M and TA. The increasing of TA amount changed the intramolecular interactions, microstructure and texture properties of M-TA-SPI gels. Compared with TA-SPI, M retarded the gastric digestion of M-TA-SPI and caused higher TA release amount in intestinal tract. In this study, M-TA-SPI was determined to be a good carrier to protect and release TA in gastrointestinal digestion. This kind of complex may have potential applications for loading polyphenols in nutraceuticals.