三聚磷酸钠对猪肉肌原纤维蛋白功能特性的影响

Effect of Sodium Tripolyphosphate on Functional Properties of Pork Myofibrillar Protein

以猪肉肌原纤维蛋白(myofibril protein,MP)为研究对象,探讨不同质量浓度三聚磷酸钠(sodiumtripolyphosphate,STP)的添加对MP乳化性、乳化稳定性、起泡性等7个功能特性指标的影响,并进行相关性分析。结果表明:随着STP质量浓度升高,MP的乳化性、乳化稳定性、起泡性、起泡稳定性、凝胶强度和凝胶保水性均呈上升趋势,表面疏水性呈下降趋势;MP的起泡性和凝胶强度在STP质量浓度为0.3 g/100 mL时最大,乳化性、表面疏水性和凝胶保水性在STP质量浓度为0.4 g/100 mL时效果最佳;MP的起泡性、起泡稳定性和乳化性呈极显著正相关(P<0.01),乳化性与乳化稳定性呈显著正相关(P<0.05),乳化性、乳化稳定性、起泡性、起泡稳定性与表面疏水性呈极显著负相关(P<0.01),与凝胶保水性呈极显著正相关(P<0.01),表面疏水性与凝胶保水性呈极显著负相关(P<0.01),表面疏水性与凝胶强度呈极显著正相关(P<0.01)。STP可以增强MP的功能特性,其质量浓度为0.3~0.4 g/100 mL时效果最佳。改善乳化性、起泡性和表面疏水性等界面性质可以增强MP的凝胶特性。

The objective of this study was to evaluate the effect of different concentrations of sodium tripolyphosphate(STP) on 7 functional characteristics of pork myofibrillar protein(MP) such as emulsifying capacity, emulsion stability and foaming characteristics, and correlation analysis was performed. The results showed that emulsifying capacity,emulsion stability, foaming property, foam stability, gel strength and water-retaining property were increased while surface hydrophobicity was decreased with increasing concentration of STP. The maximum foaming capacity and gel strength were obtained at a STP concentration of 0.3 g/100 mL, whereas the best emulsifying capacity, surface hydrophobicity, gel strength and water-retaining property were obtained at 0.4 g/100 mL. There was a significant positive correlation between foaming capacity and foam stability and emulsifying capacity(P < 0.01), and emulsifying capacity was significantly positively correlated with emulsion stability(P < 0.05). Emulsifying capacity, emulsion stability and foam stability were significantly positively correlated with surface hydrophobicity(P < 0.01) and negatively correlated with gel water-retaining property(P < 0.01). In conclusion, sodium tripolyphosphate could enhance the functional properties of myofibrillar protein and the optimum concentration was 0.3-0.4 g/100 mL. Improving the interfacial properties emulsifying capacity, foaming characteristics and surface hydrophobicity could enhance the gel properties of myofibrillar proteins.