本文研究了不同酸碱度条件对兔肉肌原纤维蛋白功能特性的影响，以及肌原纤维蛋白功能特性指标间的相关性，并通过蛋白质三级结构的变化对其机理进行初探。研究发现，随着pH逼近等电点范围，蛋白质内部芳香族氨基酸不断暴露，蛋白的三级结构展开，表面疏水性不断变大，使得蛋白质分子间疏水相互作用增加。肌原纤维蛋白结构的变化引起蛋白质溶解度下降，并且伴随着乳化活性减小以及乳化稳定性的变化。同时这种结构变化导致肌原纤维蛋白流变学特性的变化，pH减小导致剪切应力变小，并且在近等电点时，剪切应力存在明显变化。随着pH不断减小，肌源性蛋白凝胶硬度不断增大，并且在近等电点时变小；同时凝胶保水性不断下降，而凝胶白度不断增大。

 This study investigated the effects of different pH conditions on the function of myofibrillar protein in rabbit meat, the correlation between the functional indexes of myofibrillar protein and the mechanism of protein tertiary structure. It was found that, with the pH approaching the isoelectric point range, the aromatic amino acids inside the protein were exposed, the tertiary structure of the protein was unfolded, and the surface hydrophobicity became larger, which resulted in the increase of the hydrophobic interaction between the proteins. Changes in myofibrillar protein structure cause protein solubility to decrease, and accompanied by decreased emulsifying activity and changes in emulsion stability. At the same time, this structural change leads to the change of myofibrillar protein rheological properties. The decrease of pH leads to the decrease of shear stress, and the shear stress changes obviously at the near isoelectric point. With the decrease of pH, the hardness of myogenic protein gel increases, and becomes smaller at near isoelectric point. At the same time, the gel retention of gel is decreasing and the gel whiteness is increasing.