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Abstract
1. The present study compared the ability of native, heat-treated and aged turkey breast muscle proteins to undergo proteolysis by digestive tract proteases.
2. Domestic turkey toms were slaughtered under laboratory conditions. Breast muscles were excised immediately post mortem; one was placed under conditions to develop exudative meat by maintaining the muscle at 40°C for at least 30 min and the other was refrigerated under commercial conditions.
3. Meat was collected and stored for 7 d at 4°C. Breast samples removed at d 0 and d 7 were frozen and stored at −80°C until used for determination of solubility, protein surface hydrophobicity and protein oxidation through carbonyl content. Measurements of pepsin and trypsin/chymotrypsin activities were performed in vitro on myofibrillar proteins.
4. Storage increased carbonyl content in control samples while the oxidation increase was not significant in heat-treated myofibrillar protein. Hydrophobicity was not affected by storage time or treatment or protein solubility.
5. Storage significantly increased trypsin + chymotrypsin activity only in the control group. The activities of pepsin and trypsin + chymotrypsin were negatively correlated with protein surface hydrophobicity.