Journal
ASIAN-AUSTRALASIAN JOURNAL OF ANIMAL SCIENCES
Volume 32, Issue 5, Pages 721-733Publisher
ASIAN-AUSTRALASIAN ASSOC ANIMAL PRODUCTION SOC
DOI: 10.5713/ajas.18.0389
Keywords
Pale; Soft and Exudative (PSE)-like; Chicken; Actomyosin; Gel Properties; Molecular Forces
Categories
Funding
- National Natural Science Foundation of China (NSFC) [31601492]
- National Key Research and Development Program of China [2018YFD0401200]
- Key Scientific Research Project of Henan Institution of Higher Education [16A550006]
- Research Fund Project of Zhengzhou University of light industry [2015BSJJ038]
- Foundation for Young Key Teachers of Zhengzhou University of Light Industry [201711]
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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 (T-o), thermal transition temperature (T-d), storage modulus (G') and loss modulus (G ''). The turbidity, reactive sulfhydryl group of PSE-like actomyosin were higher when heated from 40 degrees C to 60 degrees C. Further heating to 80 degrees 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.
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