化学
食物蛋白
溶解度
粒径
超声波
共价键
蛋白质二级结构
吸附
大豆蛋白
食品工业
粒子(生态学)
化学工程
食品科学
有机化学
生物化学
物理化学
地质学
海洋学
工程类
声学
物理
作者
Dongjie Huang,Wenjing Li,Guannan Li,Wenyuan Zhang,Hongru Chen,Yang Jiang,Dapeng Li
标识
DOI:10.1016/j.foodhyd.2022.108056
摘要
Insect is an important source of dietary protein, and its application in the food industry has attracted attention. Tenebrio Molitor is rich in water-soluble protein, and the over-hydrophilic nature of water-soluble protein generally limits its industrial application. For the above reasons, this study systematically investigated the effect of high-intensity ultrasound (HIUS) on the physicochemical and physical characteristics of Tenebrio Molitor Protein (TMP). The results show that HIUS treatment might break the non-covalent bonds through the cavitation effect generated by the ultrasound probe, inducing the unfolding and disintegration of TMP soluble aggregates, and resulting in hydrophobic exposure and particle size reduction. HIUS optimize the physical characteristics of TMP (solubility, foamability, foam stability, emulsification, etc.) by changing its secondary/tertiary structure. Furthermore, emulsions stabilized by HIUS-treated TMP (UTMPEs) present smaller particle size and denser structure due to the changes in secondary structure, which plays a dominant role in the protein interface adsorption stabilization. The results of this study are expected to provide new guidance for better application of HIUS-treated TMP in the future food industry.
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