Effects of Acrolein Oxidization on Muscle Structure and Myofibrillar Protein Structural Properties in Large Yellow Croaker (Pseudosciaena crocea)
Article
Figures
Metrics
Preview PDF
Reference
Related
Cited by
Materials
Abstract:
In order to investigate the effects of small molecular aldehydes (among secondary lipid oxidation products) on the muscle structure and structural properties of myofibrillar proteins in large yellow croaker (Pseudosciaena crocea), the fish muscle was treated with different concentrations (0~10 mmol/L) of acrolein in an ex vivo oxidation experiment. The results showed that treatment with acrolein could lead to increased gaps between myofibers in large yellow croaker. Muscle fiber fracture and fragmentation occurred when the acrolein concentration reached 10 mmol/L, and the water-holding capacity of the fish muscle decreased when the acrolein concentration was greater than 0.1 mmol/L. The carbonyl content, bityrosine content, and surface hydrophobicity of the myofibrillar proteins increased significantly with an increase in the acrolein concentration above 0.1 mmol/L, whereas the contents of total sulfhydryl groups decreased significantly. Active sulfhydryl groups were sensitive to acrolein, and their contents decreased by 40.8% compared with the control at an acrolein concentration of 0.01 mmol/L. The SDS-PAGE results showed that acrolein oxidation could cause conjunction of some protein subunits, which formed aggregates in the area above 200 ku. In addition, the oxidation caused damage of the gel properties of the myofibrillar proteins, including decreases in the gel strength, water-holding capacity, and gel whiteness. All these results indicate that acrolein can damage the muscle structure of large yellow croaker and cause oxidation of the myofibrillar protein, thus damaging the structure and functional properties of the protein.
