Effect of animal (lamb) diet and meat storage on myofibrillar protein oxidation and in vitro digestibility

• Published in: Meat science Vol. 79; no. 4; pp. 777 - 783
• Main Authors: Santé-Lhoutellier, Véronique, Engel, Erwan, Aubry, Laurent, Gatellier, Philippe
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.08.2008; [Amsterdam]: Elsevier Science; Elsevier
• Subjects: Biological and medical sciences; carbonyl compounds; Chemical Sciences; Diet; Digestibility; digestible protein; feed concentrates; Feeding. Feeding behavior; Food industries; food storage; Fundamental and applied biological sciences. Psychology; Immunoblotting; in vitro digestibility; lamb feeding; Lamb meat; lambs; longissimus dorsi; Meat and meat product industries; meat protein; muscle protein; Myofibrillar proteins; pastures; protein aggregates; Protein oxidation; proteolysis; refrigeration; Storage; storage time; Vertebrates: anatomy and physiology, studies on body, several organs or systems; Storage; Protein oxidation; Diet; Myofibrillar proteins; Immunoblotting; Lamb meat; Digestibility; Storage protein; Meat product; In vitro; Warehousing; Food preservation; Oxidation
• ISSN: 0309-1740; 1873-4138
• DOI: 10.1016/j.meatsci.2007.11.011

Effect of pasture- or concentrate-diet on myofibrillar protein oxidation and in vitro digestibility was measured in lamb meat (M. longissimus dorsi) during a refrigerated storage of 7 days under gas permeable film. Protein oxidation was measured by the carbonyl content determined chemically using 2,4-dinitrophenylhydrazine (DNPH) and specific targets of oxidation were identified by immunoblotting. Carbonyl content significantly increased during storage and diet affected protein oxidation where animals fed concentrate showed higher carbonyl group levels than animals fed pasture. To evaluate effect of diet and storage time on protein digestibility, myofibrillar proteins were exposed to proteases of the digestive tract (pepsin, and a mixture of trypsin and α-chymotrypsin) in conditions of pH and temperature which mimic digestive process. The myofibrillar protein digestibility was not influenced by the diet. Storage time had no significant effect on myofibrillar protein susceptibility to pepsin while an important increase in digestibility by trypsin and α-chymotrypsin was detected during storage.