Insight into the effect of ultrasound treatment on the rheological properties of myofibrillar proteins based on the changes in their tertiary structure. (July 2022)

• Record Type: Journal Article
• Authors: Wang, Haifeng; Wang, Pingya; Shen, Qing; Yang, Huijuan; Xie, Hujun; Huang, Min; Zhang, Jin; Zhao, Qiaoling; Luo, Pei; Jin, Danping; Wu, Jiahui; Jian, Shikai; Chen, Xi
• Is Part Of: Food research international. Volume 157(2022)
• Publication Date: 2022-07
• Subjects: Myofibrillar protein -- Ultrasound -- Tertiary structure -- Rheology -- Schematic model -- Correlation analysis; MPs Myofibrillar proteins -- UT ultrasound treatment -- R-SH the reactive sulfhydryl content -- BPB bromophenol blue -- S0-BPB surface hydrophobicity -- UV ultraviolet–visible -- PCA principal component analysis -- Trp Tryptophan -- Tyr Tyrosine -- SAOS small amplitude oscillatory shear measurements -- LVR linear viscoelastic region; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2022.111136
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphic abstract: Highlights: UT increased the tolerance of the MPs to permanent deformation. UT improved structural rigidity of MPs. UT unfold MPs, changed the tertiary structure of MPs. There was high correlation between tertiary structure and rheological changes of MPs. Abstract: 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.