Comparison of proteolysis in native, heat-treated and aged proteins from turkey meat
Sante-Lhoutellier, V.S. | Theron, L. | Cepeda, M. | Grajales, A. | Gatellier, P.
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.
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