Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat

• Published in: Brazilian Archives of Biology and Technology Vol. 62
• Main Authors: Marchi, Denis Fabrício, Beteto, Flávia Maria, Almeida, Gleice Rocha dos Santos, Soares, Adriana Lourenço, Hernandez-Blazquez, Francisco Javier, Ida, Elza Iouko, Shimokomaki, Massami
• Format: Journal Article
• Language: English
• Published: Instituto de Tecnologia do Paraná (Tecpar) 2019
• Subjects: Collagen content; Cooking loss; Myofibrillar Fragmentation Index; Tenderness
• ISSN: 1516-8913; 1678-4324; 1678-4324
• DOI: 10.1590/1678-4324-2019180119

Abstract The aim of this work was to study the myofibril proteins and collagen fraction changes in broiler chickens PSE (pale, soft, exudative) meat during ageing and their relationship to meat quality. The results presented an increase of myofibril proteins and collagen solubility promoted by the enhanced proteases activities during storage. Ultramicroscopically, the PSE meat samples revealed intracellularly a sarcomere super contraction and lacunas within the A and I bands while Z-lines appeared very dense and fragmented in comparison to normal samples. This observation was noticed already at 4h storage while extracellularly collagen fibrils decreased visually within the endomysium only after 24h of conditioning. These results influenced the quality as the PSE meat presented better functional properties at the first hours of conditioning before further proteins degradation by proteases. Thereafter, at the later ageing stage a further disintegration of the abnormal meat structure would affect the meat functional properties.