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Br Poult Sci. 2008 May;49(3):308-14. doi: 10.1080/00071660802146006.

Comparison of proteolysis in native, heat-treated and aged proteins from turkey meat.

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1
INRA, UR QuaPA370, Saint Genès Champanelle, France. veronique.sante@clermont.inra.fr

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 degrees 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 degrees C. Breast samples removed at d 0 and d 7 were frozen and stored at -80 degrees 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.

PMID:
18568755
DOI:
10.1080/00071660802146006
[Indexed for MEDLINE]
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