Comparative study of thermal gelation properties and molecular forces of actomyosin extracted from normal and pale, soft and exudative-like chicken breast meat

• Main Authors: Ke Li, Jun-Ya Liu, Lei Fu, Ying-Ying Zhao, Yan-Hong Bai
• Format: Article
• Language: English
• Published: Asian-Australasian Association of Animal Production Societies 2019-05-01
• Series: Asian-Australasian Journal of Animal Sciences
• Subjects: Pale; Soft and Exudative (PSE)-like; Chicken; Actomyosin; Gel Properties; Molecular Forces
• Online Access: http://www.ajas.info/upload/pdf/ajas-18-0389.pdf

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 pale, soft and exudative [PSE]-like) during heating process to further improve the understanding of the variations of functional properties between normal and PSE-like chicken breast meat. Methods Actomyosin was 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. Results Sodium dodecyl sulphate-polyacrylamide gel electrophoresis 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). Conclusion 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.