Abstract
In this study, structural characteristics and formation mechanism of Mesona chinensis polysaccharide (MCP)-whey protein isolate (WPI) gels including group and molecular changes, intermolecular forces, crystallinity, and moisture migration were investigated under pH shifting conditions. Results showed that MCP and WPI formed a stable gel at pH 10. The free sulfhydryl groups and surface hydrophobicity of the MCP-WPI gels increased with the increasing pH. Hydrophobic and hydrogen bond interactions were the main molecular forces involved in the MCP-WPI gels, and electrostatic interactions and disulfide bonds played a complementary role. The pH conditions evidently influenced the secondary conformational structure of MCP-WPI gels. Molecular weight and X-ray diffraction (XRD) analysis indicated the formation of a hypocrystalline complex with molecular interaction. In addition, low-field magnetometry (LF-NMR) results showed that the T2 values decreased with increasing pH, indicating that water and gel matrix had the highest interactions at pH 10.
Published Version
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