Solubilization strategy of myofibrillar proteins in low-ionic media (prototype soup): The effect of high-intensity ultrasound combined with non-covalent or covalent modification of polyphenols on myosin molecular assembly

IF 8.5 1区农林科学 Q1 CHEMISTRY, APPLIED Food Chemistry Pub Date : 2023-10-11 DOI:10.1016/j.foodchem.2023.137701

Chao Zhang, Ziyi Wang, Qian Liu, Qian Chen, Fangda Sun, Haotian Liu, Baohua Kong

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Abstract

This study investigated the effect of (−)-Epigallocatechin-3-gallate (EGCG) non-covalent/covalent grafting onto myofibrillar protein (MP) by high-intensity ultrasound (HIU) on its water-solubility and filament forming behavior. The results showed that the introduction of EGCG, especially in the case of covalent grafting, could inhibit the molecular assembly of myosin and improve the MP water solubility from 2.7% to 53.1% (P < 0.05). The HIU pretreatment provided more opportunities for EGCG grafting onto the ultrasound-treated protein (UMP) by disrupting the filamentous polymerization of myosin and thus further facilitated MP dissolution. Additionally, compared with the UMP-EGCG non-covalent complexes, the covalent complexes with a yellow appearance exhibited a higher absolute zeta potential (35.9 mV) and a lower particle size (53.7 μm) (P < 0.05). Overall, the combination of HIU pretreatment and EGCG covalent modification may provide a promising method for improving the solubility and processing properties of MP in low ionic media (prototype soup).

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肌原纤维蛋白在低离子介质中的溶解策略（原型汤）：高强度超声结合多酚的非共价或共价修饰对肌球蛋白分子组装的影响。

研究了高强度超声（HIU）将（-）-表没食子儿茶素-3-没食子酸酯（EGCG）非共价/共价接枝到肌原纤维蛋白（MP）上对其水溶性和成丝行为的影响。结果表明，EGCG的引入，特别是在共价接枝的情况下，可以抑制肌球蛋白的分子组装，并将MP的水溶性从2.7%提高到53.1%（P

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来源期刊

Food Chemistry 工程技术-食品科技

CiteScore

16.30

自引率

10.20%

发文量

3130

审稿时长

122 days

期刊介绍： Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.