肌原纤维
热稳定性
纹理(宇宙学)
微观结构
化学
蛋白质聚集
二硫键
化学工程
生物物理学
结晶学
有机化学
生物化学
人工智能
计算机科学
工程类
图像(数学)
生物
作者
Bo Chen,Kai Zhou,Yu Wang,Yong Xie,Zhaoming Wang,Peijun Li,Baocai Xu
出处
期刊:Food Chemistry
[Elsevier]
日期:2020-05-30
卷期号:330: 127186-127186
被引量:125
标识
DOI:10.1016/j.foodchem.2020.127186
摘要
The present study aimed to illuminate the mechanism of textural deterioration of MP gels induced by high temperature treatments (75-95 °C, 20 min). Measurements of textural properties showed that the decreased thermal stability is responsible for the gel texture. Analysis of the microstructure of MP gel showed that the over-aggregation of MP was strictly related to the gel quality loss. Further investigations on protein structures indicated that the proteins tended to be more stretched in higher temperature treatments, leading to an increase in disulfide bonds and a reduction in the noncovalent interactions, promoting the over-aggregation of protein. To conclude, high temperature-induced textural deterioration of MP gel was initialized by the dramatic changes of protein structures during heat treatment, which decreased thermal stability of MP gels due to the over-aggregation of MP molecules. Once the altered thermal stability was insufficient to resist the over-heating, such deterioration would occur.
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