高压处理对肌原纤维蛋白构象和凝胶特性的影响
Effects of high pressure modification on conformation and gelation properties of myofibrillar protein.
作者信息
Zhang Ziye, Yang Yuling, Zhou Peng, Zhang Xing, Wang Jingyu
机构信息
College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, PR China; State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, PR China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, Jiangsu Province 214122, PR China.
College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, PR China.
出版信息
Food Chem. 2017 Feb 15;217:678-686. doi: 10.1016/j.foodchem.2016.09.040. Epub 2016 Sep 7.
The effects of high pressure (HP) treatment (100-500MPa) on conformation and gelation properties of myofibrillar protein (MP) were investigated. As pressure increased (0.1-500MPa), α-helix and β-sheet changed into random coil and β-turn, proteins unfolded to expose interior hydrophobic and sulfhydryl groups, therefore surface hydrophobicity and formation of disulfide bonds were strengthened. At 200MPa, protein solubility and gel hardness reached their maximum value, particle size had minimum value, and gel microstructure was dense and uniform. DSC data showed that actin and myosin completely denatured at 300MPa and 400MPa, respectively. Rheological modulus (G' and G″) of HP-treated MP decreased as pressure increased during thermal gelation. Moderate HP treatment (≦200MPa) strengthened gelation properties of MP, while stronger HP treatment (⩾300MPa) weakened the gelation properties. 200MPa was the optimum pressure level for modifying MP conformation to improve its gelation properties.
研究了高压（HP）处理（100 - 500MPa）对肌原纤维蛋白（MP）构象和凝胶化特性的影响。随着压力升高（0.1 - 500MPa），α-螺旋和β-折叠转变为无规卷曲和β-转角，蛋白质展开以暴露内部的疏水基团和巯基，因此表面疏水性和二硫键的形成得到增强。在200MPa时，蛋白质溶解度和凝胶硬度达到最大值，粒径达到最小值，且凝胶微观结构致密均匀。差示扫描量热法（DSC）数据表明，肌动蛋白和肌球蛋白分别在300MPa和400MPa时完全变性。在热凝胶化过程中，经高压处理的MP的流变模量（G'和G″）随压力升高而降低。适度的高压处理（≤200MPa）增强了MP的凝胶化特性，而更强的高压处理（≥300MPa）则削弱了凝胶化特性。200MPa是改变MP构象以改善其凝胶化特性的最佳压力水平。
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