Isoelectric solubilization/precipitation processing modified sarcoplasmic protein from pale, soft, exudative-like chicken meat
Isoelectric solubilization/precipitation processing modified sarcoplasmic protein from pale, soft, exudative-like chicken meat
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等电溶解/沉淀处理来自苍白、柔软、渗出状鸡肉的改性肌浆蛋白
DOI：
10.1016/j.foodchem.2019.02.085
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发表时间：
2019
期刊：
影响因子：
8.8
通讯作者：
Zhou Guanghong
中科院分区：
文献类型：
--
作者：
Zhao Xue;Xing Tong;Wang Yingyao;Xu Xinglian;Zhou Guanghong
采用等电增溶/沉淀法对苍白、柔软、渗出状鸡胸肉中的肌浆蛋白进行了改性。修饰后，肌浆蛋白获得了比未处理的样品更大的颗粒分布，表明严重的聚集。等电增溶/沉淀处理的肌浆蛋白聚集体表现出絮凝和无定形的形状稳定的疏水相互作用。碱处理的肌浆蛋白的疏水相互作用在加热过程中是相对恒定的，而它们显着增加在未经处理的样品。碱处理的肌浆蛋白能提高肌原纤维蛋白的凝胶特性，具有较高的断裂力和较低的蒸煮损失。根据我们的研究结果，假设碱处理的肌浆蛋白可能不干扰肌原纤维蛋白的凝胶化行为，但确实填充了三维网络的孔隙，从而增强了其凝胶弹性。总的来说，碱处理的肌浆蛋白表现出改善肌原纤维蛋白凝胶化特性的潜力。
The sarcoplasmic protein from pale, soft and exudative -like chicken breast meat was modified using an isoelectric solubilization/precipitation process. After the modification, the sarcoplasmic protein obtained a larger particle distribution than the nontreated sample, indicating a severe aggregation. The isoelectric solubilization/precipitation-treated sarcoplasmic protein aggregates exhibited a flocculated and amorphous shape stabilized by the hydrophobic interactions. The hydrophobic interactions of alkali-treated sarcoplasmic proteins were relatively constant during heating, while they dramatically increased in nontreated sample. The alkali-treated sarcoplasmic protein could promote myofibrillar protein gelation properties, as proved by the higher breaking force and lower cooking loss. According to our results, it is hypothesized that the alkali-treated sarcoplasmic protein likely does not interfere in the gelation behavior of myofibrillar protein but does fill in the pores of the three-dimensional network, thereby strengthening its gelation elasticity. Overall, the alkali-treated sarcoplasmic protein exhibits the potential to improve the myofibrillar protein gelation properties.