School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, China; Engineering Research Center of Bio-process, Ministry of Education, Hefei University of Technology, Hefei 230601, China; Food Laboratory of Zhongyuan, Luohe 462300, Henan, China.
School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, China; Engineering Research Center of Bio-process, Ministry of Education, Hefei University of Technology, Hefei 230601, China.
Food Chem. 2023 Jun 30;412:135472. doi: 10.1016/j.foodchem.2023.135472. Epub 2023 Jan 11.
The study presented the effects of modulating the hydrophobic interaction and disulfide bond on the properties of myofibrillar protein (MP) emulsion gels at high temperature (95 °C) and the differentiation on the contribution of non-covalent (hydrophobic interaction) and covalent intermolecular interactions (disulfide bond) to the properties of interfacial protein films were also determined. The hydrophobic interactions among MP were modulated by the addition of octenyl succinic anhydride (OSA), and the disulfide bonds were modulated by the SH/SS exchange reactions mediated by GSH. The results showed that the MP emulsion gel properties at 95 °C were improved by modulating the hydrophobic interaction or disulfide bonds, and the dynamic interfacial adsorption of MP and dissipation quartz crystal microbalance experiments showed the interfacial adsorption pattens of protein were also changed. In addition, the hydrophobic interactions putted emphasis on improving the gel matrix, whereas the disulfide bonds focused on increasing the stiffness of interfacial protein films.
该研究探讨了在高温（95°C）下调节疏水性相互作用和二硫键对肌原纤维蛋白（MP）乳液凝胶特性的影响，并确定了非共价（疏水性相互作用）和共价分子间相互作用（二硫键）对界面蛋白膜特性的贡献差异。通过添加辛烯基琥珀酸酐（OSA）来调节 MP 之间的疏水性相互作用，通过 GSH 介导的 SH/SS 交换反应来调节二硫键。结果表明，通过调节疏水性相互作用或二硫键可以改善 95°C 下的 MP 乳液凝胶特性，并且 MP 的动态界面吸附和耗散石英晶体微天平实验表明，蛋白质的界面吸附模式也发生了变化。此外，疏水性相互作用侧重于改善凝胶基质，而二硫键则侧重于增加界面蛋白膜的刚性。
