高压均质处理实现骨骼肌肌原纤维蛋白的水溶解机制及其新型加工特性研究

肉中丰富蛋白质受制于其在水或低离子强度条件下的低溶解性，导致利用程度较低，而本课题以骨骼肌肌原纤维蛋白（MP）为研究对象，通过应用高压均质蛋白改性技术，研究不同高压均质条件、离子强度、pH对MP溶解性的影响，以优化肌肉蛋白其水溶解性的工艺条件；在此基础上，利用酶标仪、圆二色谱、红外光谱仪等测定表面官能团含量以及分子构象变化，利用激光光散射仪、密度仪和差示热量扫描仪等测定蛋白分子聚集和热力学变化，利用酶解、SDS-PAGE和质谱等技术测定蛋白水溶解的关键结构域、对实现蛋白水溶解起重要作用的分子片段，利用化学修饰法测定化学作用力对改性蛋白热特性变化的贡献，以阐明高压均质实现蛋白水溶解机理并揭示高压均质改性蛋白的热特性变化规律；最后探索在此条件下改性蛋白粉的物化性质和溶解、乳化等新型加工特性，以期进一步丰富骨骼肌MP在低离子强度下溶解的理论研究，为开发新型肉蛋白产品提供理论指导。

Meat is a nutrient-rich food. However, Meat proteins have not been fully utilized because of the low solubility of myofibrillar proteins (MP) in water or low ionic strength solutions. In the present project, the skeletal muscle MP regarded as the research materials are subjected to protein modification by high pressure homogenization (HPH) technology. To optimize the process parameters in solubilization muscle proteins in water, the effects of different homogenization conditions, ionic strengths and pHs on the solubility of MP will be investigated. Then, to elucidate the mechanism of protein solubilized in water by the HPH and to reveal thermal characteristics of HPH treated MP, the surface functional group content and molecular conformational changes of protein will be determined by using the microplate, circular dichroism, and infrared spectroscopy, the determination of protein molecular aggregation and thermodynamic changes will be conducted by using laser light scattering instrument, density measurement and differential scanning calorimetry determination, the water soluble protein domain and the key subfragments of protein molecule contributing to the water solubility are going to be studied by using enzyme hydrolysis, SDS-PAGE and mass spectrometry determination, the chemical interactions within the proteins will be tested by the chemical modification method. Finally, the physicochemical properties and functional properties such as solubility and emulsify property of HPH modified MP powder under certain conditions are going to be explored. Overall, the research results of this task will enrich the theory of skeletal muscle MPs solubilized in low ionic strength and provide theoretic guidelines for the R&D of new meat protein products.