State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; College of Food Science and Engineering, Hainan University, Haikou 570228, China.
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China.
Food Chem. 2021 Sep 1;355:129650. doi: 10.1016/j.foodchem.2021.129650. Epub 2021 Mar 23.
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 T values decreased with increasing pH, indicating that water and gel matrix had the highest interactions at pH 10.
本研究探讨了在 pH 值变化条件下,花椒多糖(MCP)-乳清蛋白分离物(WPI)凝胶的结构特征和形成机制,包括基团和分子变化、分子间作用力、结晶度和水分迁移。结果表明,MCP 和 WPI 在 pH 值为 10 时形成稳定的凝胶。MCP-WPI 凝胶的游离巯基和表面疏水性随 pH 值的增加而增加。疏水相互作用和氢键是 MCP-WPI 凝胶的主要分子作用力,静电相互作用和二硫键起补充作用。pH 值明显影响 MCP-WPI 凝胶的二级构象。分子量和 X 射线衍射(XRD)分析表明,形成了具有分子相互作用的低结晶复合物。此外,低场磁共振(LF-NMR)结果表明,T 值随 pH 值的增加而降低,表明在 pH 值为 10 时水和凝胶基质的相互作用最大。