Protein oxidation and subsequent changes in chicken breast and thigh meats during long-term frozen storage
In this study, protein oxidation and subsequent changes were evaluated during the long-term frozen storage of chicken meat cuts. Boneless and skinless chicken breast and thigh meat cuts were packaged, frozen, and stored at −18 °C for 6 months, whereas physicochemical analysis and electrophoretic protein profile were evaluated every 1 month. In breast and thigh meats, carbonyl content was noted to increase, whereas sulphydryl content decreased during frozen storage (p<0.05). A significant decrease in protein solubility and water holding capacity (p<0.05) was also determined due to denaturation and aggregation of proteins as a result of protein oxidation. Myofibrillar proteins, particularly myosin heavy chain, were identified to be more susceptible to oxidation although no notable changes were determined in sarcoplasmic protein pattern. In general, significant proteolytic changes were particularly noted from the third month of storage onward. This could be a useful finding in order to make a decision for shelf life and thus minimize undesirable quality changes in chicken meats. Additionally, strong correlations were noted between the examined quality parameters.