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Asian-Australas J Anim Sci > Accepted Articles
DOI: https://doi.org/10.5713/ajas.18.0389    [Accepted] Published online September 13, 2018.
Comparative study of thermal gelation properties and molecular forces of actomyosin extracted from normal and pale, soft and exudative (PSE)-like chicken breast meat
Ke Li1,*, Jun-Ya Liu1, Lei Fu1, Ying-Ying Zhao1, Yan-Hong Bai1
College of Food and Bioengineering, Zhengzhou University of Light Industry, Henan Collaborative Innovation Center for Food Production and Safety, Henan Key Laboratory of Cold Chain Food Quality and Safety Control, Zhengzhou, 450001, China
Correspondence:  Ke Li, Tel: +86-18736067558, Fax: +86-0371-86609632, Email: xc_like@163.com
Received: 22 May 2018   • Revised: 11 July 2018   • Accepted: 28 August 2018
Objective: The objectives of this study were to investigate the thermal gelation properties and molecular forces of actomyosin extracted from two classes of chicken breast meat qualities (normal and PSE-like) during heating process to further improve the understanding of the variations of functional properties between normal and PSE-like chicken breast meat.


Actomyosin were extracted from normal and PSE-like chicken breast meat and the gel strength, water-holding capacity (WHC), protein loss, particle size and distribution, dynamic rheology and protein thermal stability were determined, then turbidity, active sulfhydryl group contents, hydrophobicity and molecular forces during thermal-induced gelling formation were comparatively studied.


SDS-PAGE showed that protein profiles of actomyosin extracted from normal and PSE-like meat were not significantly different (P>0.05). Compared with normal actomyosin, PSE-like actomyosin had lower gel strength, WHC, particle size, less protein content involved in thermal gelation forming (P<0.05), and reduced onset temperature (To), thermal transition temperature (Td), storage modulus (G') and loss modulus (G"). The turbidity, reactive sulfhydryl group of PSE-like actomyosin were higher when heated from 40°C to 60°C. Further heating to 80°C had lower transition from reactive sulfhydryl group into a disulfide bond and surface hydrophobicity. Molecular forces showed that hydrophobic interaction was the main force for heat-induced gel formation while both ionic and hydrogen bonds were different significantly between normal and PSE-like actomyosin (P<0.05).
These changes in chemical groups and inter-molecular bonds affected protein-protein interaction and protein-water interaction and contributed to the inferior thermal gelation properties of PSE-like meat.
Keywords: PSE-like; Chicken; Actomyosin; Gel properties; Molecular forces

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