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超声辅助海藻酸钠处理对鸡胸肉品质的影响:肌原纤维蛋白结构和凝胶特性的作用。

Effects of the structure and gel properties of myofibrillar protein on chicken breast quality treated with ultrasound-assisted potassium alginate.

机构信息

Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, PR China.

Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, PR China; School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Rd, 212013 Zhenjiang, Jiangsu, PR China; Key Lab of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, 210014, China.

出版信息

Food Chem. 2021 Oct 1;358:129873. doi: 10.1016/j.foodchem.2021.129873. Epub 2021 Apr 20.

DOI:10.1016/j.foodchem.2021.129873
PMID:33933962
Abstract

This paper aimed to evaluate the effects of the structure and gel properties of myofibrillar protein (MP) on 300-days-old chicken breast quality treated with ultrasound (300 W) and low addition (4 mg/mL) of potassium alginate (UPA). The results showed that UPA group exhibited lower liquid loss and optimized texture correlated with the formed water barrier and damaged myofibrils. UPA reduced the MP size and increased its solubility, and the decreased myosin thermostability and dissociated actomyosin reduced heating time for improved texture. UPA improved the gel strength, elastic modulus and ordered-arrangement of network. During gelation, the aggregation of myosin head was weakened and cross-linking of myosin tail and PA molecules was enhanced by hydrophobic interactions. UPA further inhibited the formation of disulfide bonds of myosin head and increased gel firmness. The lower myosin gelling temperature thus accelerated gel formation, and enhanced protein association with PA molecules facilitated the better gel performance.

摘要

本研究旨在评估超声(300W)和低添加量(4mg/mL)海藻酸钠(UPA)处理对 300 日龄鸡胸肉品质的影响。结果表明,UPA 组的汁液损失较低,质地得到优化,这与形成的水屏障和受损的肌原纤维有关。UPA 降低了肌球蛋白的大小并增加了其溶解度,降低的肌球蛋白热稳定性和解聚的肌动球蛋白缩短了加热时间,从而改善了质地。UPA 提高了凝胶强度、弹性模量和网络有序排列。在凝胶形成过程中,通过疏水相互作用,弱化了肌球蛋白头部的聚集,增强了肌球蛋白尾部和 PA 分子的交联。UPA 进一步抑制了肌球蛋白头部二硫键的形成,增加了凝胶硬度。较低的肌球蛋白胶凝温度因此加速了凝胶形成,并且蛋白质与 PA 分子的缔合促进了更好的凝胶性能。

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