Wang Qian, Jiao Xidong, Yan Bowen, Meng Linglu, Cao Hongwei, Huang Jianlian, Zhao Jianxin, Zhang Hao, Chen Wei, Fan Daming
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China; Fujian Provincial Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing, Xiamen 361022, China; Fujian Anjoyfood Share Co. Ltd., Xiamen 361022, China.
Food Chem. 2021 Sep 30;357:129745. doi: 10.1016/j.foodchem.2021.129745. Epub 2021 Apr 20.
This work was aimed to compare the effect of microwave (MW) heating on the cathepsin L (Cat L)-induced degradation of myofibrillar protein (MP) gels with that of water bath (WB) heating. First, Cat L from silver carp was purified and determined to be 45 kDa. The gel strength of the MW-heated MP gels were significantly higher than those of the WB-heated when Cat L was added (P < 0.05). The gel electrophoresis pattern and scanning electron microscopy analysis indicated that MW heating inhibited the Cat l-induced hydrolysis of MP gels. In addition, the number of sulfhydryl groups and surface hydrophobicity of MW-heated gels were lower than those of WB-heated gels when Cat L was added. These results indicated that MW heating could effectively weaken the degradation of Cat L on MP gels by manipulating disulfide bonds and hydrophobic amino acids, resulting in good gel properties and a compact protein network.
本研究旨在比较微波（MW）加热与水浴（WB）加热对组织蛋白酶L（Cat L）诱导的肌原纤维蛋白（MP）凝胶降解的影响。首先，对鲢鱼中的组织蛋白酶L进行纯化，测定其分子量为45 kDa。添加Cat L时，MW加热的MP凝胶的凝胶强度显著高于WB加热的凝胶（P < 0.05）。凝胶电泳图谱和扫描电子显微镜分析表明，MW加热抑制了Cat L诱导的MP凝胶水解。此外，添加Cat L时，MW加热凝胶的巯基数量和表面疏水性低于WB加热凝胶。这些结果表明，MW加热可通过调控二硫键和疏水氨基酸有效减弱Cat L对MP凝胶的降解，从而产生良好的凝胶特性和紧密的蛋白质网络。
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