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Insight into the effect of ultrasound treatment on the rheological properties of myofibrillar proteins based on the changes in their tertiary structure

文献类型： 外文期刊

作者： Wang, Haifeng 1 ; Wang, Pingya 2 ; Shen, Qing 1 ; Yang, Huijuan 3 ; Xie, Hujun 1 ; Huang, Min 1 ; Zhang, Jin 4 ; Zhao, Qiaoling 2 ; Luo, Pei 5 ; Jin, Danping 1 ; Wu, Jiahui 1 ; Jian, Shikai 1 ; Chen, Xi 6 ;

作者机构： 1.Zhejiang Gongshang Univ, Inst Seafood, Collaborat Innovat Ctr Seafood Deep Proc, Zhejiang Prov Joint Key Lab Aquat Prod Proc, Hangzhou 310012, Peoples R China

2.Zhoushan Inst Food & Drug Control, Zhoushan 316000, Peoples R China

3.China Jiliang Univ, Coll Standardizat, Hangzhou 310018, Peoples R China

4.Zhejiang Acad Agr Sci, Hangzhou 310021, Peoples R China

5.Macau Univ Sci & Technol, Fac Pharm, State Key Labs Qual Res Chinese Med, Macau 999078, Peoples R China

6.Zhejiang Prov Peoples Hosp, Affiliated Peoples Hosp, Hangzhou Med Coll, Ctr Gen Practice Med,Dep Gen Practice Med, Hangzhou 310014, Zhejiang, Peoples R China

关键词： Myofibrillar protein; Ultrasound; Tertiary structure; Rheology; Schematic model; Correlation analysis

期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：7.425； 五年影响因子：7.716 ）

ISSN： 0963-9969

年卷期： 2022 年 157 卷

页码：

收录情况： SCI

摘要： This was the first study to perform correlation analysis to determine the relationships between tertiary structural and rheological properties of the myofibrillar proteins (MPs) under ultrasound treatment (UT, frequency 20 kHz, power 500 W, intensity 30 %) for 0, 2, 4, 6, 8, and 10 min. The objectives of this study were to 1) characterize the changes of the small and large deformation rheological properties of MPs based on the tertiary structural changes; 2) determine relationships of rheological property, tertiary structural changes, and UT time. The results showed that UT could enhance the structural rigidity and the resistance of the system to permanent deformation observed in rheological tests. Besides, UT could unfold MPs, expose more hydrophobic amino acid residues to increase the surface hydrophobicity (S0-BPB), destroy disulfide bonds to increase the content of reactive sulfhydryl content (R-SH). The correlation analysis showed that the rheological properties of MPs could be improved by UT with a longer treatment time (0-10 min), while inevitably and significantly changing the tertiary structure of MPs (p < 0.05). These findings suggested that UT might be effective in the food-processing industry to change the structure of proteins and improve rheological properties.

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