Skip to main content
ARS Home » Southeast Area » Athens, Georgia » U.S. National Poultry Research Center » Quality Safety and Assessment Research » Research » Publications at this Location » Publication #363118

Research Project: Assessment and Improvement of Poultry Meat, Egg, and Feed Quality

Location: Quality Safety and Assessment Research

Title: Effect of Spaghetti meat abnormality on the muscle protein composition of broiler breast meat

Author
item Bowker, Brian
item TASONIERO, GIULIA - Oak Ridge Institute For Science And Education (ORISE)
item Zhuang, Hong

Submitted to: Poultry Science Association Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 4/30/2019
Publication Date: 7/15/2019
Citation: Bowker, B.C., Tasoniero, G., Zhuang, H. 2019. Effect of Spaghetti meat abnormality on the muscle protein composition of broiler breast meat. Poultry Science Association Meeting Abstract. https://doi.org/10.1016/j.psj.2019.10.069.
DOI: https://doi.org/10.1016/j.psj.2019.10.069

Interpretive Summary:

Technical Abstract: Recent data suggests that the spaghetti meat (SM) myopathy observed in broiler pectoralis major muscle impairs meat quality and functionality; however, the impact of the myopathy on muscle protein composition is unknown. The objective of this study was to determine the effects of SM on protein characteristics and profiles of broiler breast meat. Breast fillets (30 normal (N), 30 SM) were collected from a commercial processing plant at 3 h postmortem and stored overnight at 4°C. Exudate was collected and analysed for protein content and SDS-PAGE protein profiles. Fillets (10 N, 10 SM) were cut into superficial and deep layers. Muscle protein fractions (myofibrillar and sarcoplasmic) were isolated and analysed using SDS-PAGE. Protein solubility and content were measured. The effects of muscle condition, layer, and their interaction were analysed using a 2-way ANOVA. SM fillets had lower protein content than N fillets (P<0.0001) in the superficial layer of the muscle. Myofibrillar protein solubility was lower in SM fillets than N fillets (P<0.001). Sarcoplasmic protein solubility was lower in the superficial layer of the muscle compared to the deep layer (P<0.0001). Although the protein concentration of the exudate from N and SM fillets was similar, the SM fillets lost more protein due to having a greater (P<0.05) drip loss than SM fillets (N=1.22 vs SM=1.44%; P=0.0131). Electrophoretic profiles of exudate proteins were generally similar between N and SM fillets; however, the relative abundance of protein bands corresponding to 34 kDa (lactate dehydrogenase), 47 kDa (enolase), 67 kDa, and 71 kDa were different between N and SM fillets (P<0.05). With regards to the sarcoplasmic protein fraction, muscle layer influenced (P<0.05) relative abundance of 5 proteins. The SM condition did not have a strong impact on the sarcoplasmic protein profile. For the myofibrillar fraction of the muscle, SM exhibited a lower relative abundance of a 73 kDa protein (P<0.01). Muscle layer significantly influenced the relative abundance of myofibrillar protein bands corresponding to 25 kDa and a high molecular weight protein (>250 kDa). In N fillets the relative abundance of the protein band corresponding to 100 kDa (a-actinin) was similar between the deep and superficial layers of the muscle. However, in SM fillets the relative abundance of the 100 kDa myofibrillar protein band was lower (P<0.05) in the superficial layer of the muscle compared to the deep layer. Overall data suggest that although the SM condition influences the total amount and functionality of proteins in the muscle, the sarcoplasmic and myofibrillar protein profiles in SM are similar to normal breast meat.