Research on the emulsifying and physicochemical characteristics of myofibrillar protein from several species meat | 不同种类肉肌原纤维蛋白乳化及理化特性的研究

中国人. 比较了3种肉(猪肉、牛肉和鸡肉)肌原纤维蛋白的乳化及理化特性的差异。结果表明:在1~8 mg・mL-1的蛋白质质量浓度范围内,3种肉的溶解度和乳化能力随质量浓度的增加而增大,但当质量浓度大于8 mg・mL-1时,两者的变化不显著。随着蛋白质质量浓度的增加,3种肉的黏度显著增大(P0.05),而乳化活性指数降低。当蛋白质质量浓度小于5 mg・mL-1时,乳化稳定性指数的变化不明显;当质量浓度大于5 mg・mL-1时,乳化稳定性指数随质量浓度的增加而增大。3种肉中,除蛋白质质量浓度为10 mg・mL-1时鸡肉与猪肉的乳化活性指数没有显著性差异外,在同一蛋白质质量浓度下,鸡肉的各项乳化及理化指标均显著高于其他2种肉,牛肉最低(P0.05),但鸡肉的表面疏水性最低(P0.05),牛肉最高。乳化能力与溶解度呈极显著正相关(P0.01),并受表面疏水性的影响。同时,乳化稳定性指数与黏度也极显著正相关(P0.01)。

英语. The investigation was undertaken to compare the emulsifying and physicochemical properties of myofibrillar protein from several species meat(pork,chicken and beef).The solubility and emulsifying capacity of three kinds of meat increased with the increment of protein concentration which changed from 1 to 8 mg・mL-1,but the change of the two indexes was not significant when the protein concentration was higher than 8 mg・mL-1.The viscosity significantly increased with the increment of protein concentration(P0.05),but the emulsifying activity index decreased with the increment of protein concentration.When the protein concentration was lower than 5 mg・mL-1,the change of the emulsifying stability index was not obvious.When the protein concentration was higher than 5 mg・mL-1,the emulsifying stability index increased with the increment of protein concentration.Under the same protein concentration,the emulsifying and physicochemical properties of chicken were higher than the other two kinds of meat,and pork was higher than beef(P0.05),except that the emulsifying activity index of chicken and pork had not significant difference at 10 mg・mL-1 protein concentration.The surface hydrophobicity of chicken was the lowest,and beef was higher than the other two kinds of meat(P0.05).There was a significant positive correlation between emulsifying capacity and solubility(P0.01),as well as the correlation between emulsifying stability index and viscosity(P0.01),and emulsifying capacity was influenced by the surface hydrophobicity.