花生浓缩蛋白对鸡胸肉盐溶蛋白热诱导凝胶性能的影响

本文研究了花生浓缩蛋白对鸡胸肉盐溶蛋白热诱导凝胶性能的影响。对添加花生浓缩蛋白后的鸡胸肉盐溶蛋白热诱导凝胶的质构特性、动态流变特性以及热变特性进行测定并通过扫描电镜观察其微观结构。结果表明，添加花生浓缩蛋白后，鸡胸肉盐溶蛋白热诱导凝胶性能得以改善。当添加量为2.5%时，凝胶硬度及强度达到最大，最大值分别为52.5 g、93.02 g?cm；凝胶的储能模量G’显著提高(P<0.05)，其损耗角正切值tanδ明显降低(P<0.05 )；凝胶的变性温度(Tmax)及变性焓(ΔH)显著提高(P<0.05)，当添加量为3.5%时，Tmax1、Tmax2、Tmax3和ΔH增至最大，分别为54.02 ℃、65.02 ℃、76.52 ℃、0.694 J/g；凝胶微观的三维网络结构更加紧密、有序，蛋白质交联度更高。因此，花生浓缩蛋白可以有效改善鸡胸肉盐溶蛋白热诱导凝胶硬度和强度、弹性、热稳定性以及微观结构等特性。
The effects of alcohol-leached peanut protein concentrate on heat-induced gel properties of chicken breast muscle salt-soluble proteins were examined. With the addition of alcohol-leached peanut protein concentrate, the texture properties, dynamic rheological properties, and thermal properties of the heat-induced gel of chicken breast muscle salt-soluble proteins were determined, and its microstructure was observed by scanning electron microscopy (SEM). The results showed that after adding alcohol-leached peanut protein concentrate, the heat-induced gel properties of chicken breast muscle salt-soluble proteins were improved. When the amount of alcohol-leached peanut protein concentrate was 2.5%, the maximum gel hardness and strength were reached, and they were 52.5 g and 93.02 g × cm, respectively. The storage modulus G’ was increased significantly (P < 0.05), and loss tangent value (tanδ) was decreased significantly (P < 0.05). Transition temperatures (Tmax) and enthalpy of denaturation (ΔH) of heat-induced gel were increased significantly (P < 0.05). With the addition of 3.5% alcohol-leached peanut protein concentrate, three transition temperatures (Tmax1, Tmax2, and Tmax3) and ΔH of heat-induced gel were maximally increased, and the maximum values were 54.02 ℃, 65.02 ℃, 76.52 ℃, and 0.694 J/g, respectively. Three-dimensional network microstructure of heat-induced gel with the addition of alcohol-leached peanut protein concentrate was even more compact and orderly, and the crosslinking degree between proteins became higher. Therefore, alcohol-leached peanut protein concentrate can effectively improve hardness, strength, elasticity, thermal stability, microstructure and other heat-induced gel properties of chicken breast muscle salt-soluble proteins.