Comparison of proteolysis in native, heat-treated and aged proteins from turkey meat Article uri icon

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. © 2008 British Poultry Science Ltd.
  • 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 %2b chymotrypsin activity only in the control group. The activities of pepsin and trypsin %2b chymotrypsin were negatively correlated with protein surface hydrophobicity. © 2008 British Poultry Science Ltd.

publication date

  • 2008-01-01