Relationship between water-holding capacity and protein denaturation in broiler breast meat1

Comparison of protein degradation, protein oxidation, and μ-calpain activation between pale, soft, and exudative and red, firm, and nonexudative pork during postmortem aging1

(2014) Y. Yin et al.   JOURNAL OF ANIMAL SCIENCE

Modeling as a research tool in poultry science

(2014) R. M. Gous   POULTRY SCIENCE

Postmortem aging and freezing and thawing storage enhance ability of early deboned chicken pectoralis major muscle to hold added salt water

(2012) H. Zhuang et al.   POULTRY SCIENCE

Occurrence and Characterization of Pale, Soft, Exudative-Like Broiler Muscle Commercially Produced in China

(2012) Xue-shen ZHU et al.   Journal of Integrative Agriculture

Post mortem development of meat quality as related to changes in cytoskeletal proteins of chicken muscles

(2011) J. Tomaszewska-Gras et al.   BRITISH POULTRY SCIENCE

High post-mortem temperature combined with rapid glycolysis induces phosphorylase denaturation and produces pale and exudative characteristics in broiler Pectoralis major muscles

(2011) Xueshen Zhu et al.   MEAT SCIENCE

The roles of the actin-myosin interaction and proteolysis in tenderization during the aging of chicken muscle

(2011) S. Li et al.   POULTRY SCIENCE

Effect of ultimate pH and freezing on the biochemical properties of proteins in turkey breast meat

(2010) Jacky T.Y. Chan et al.   FOOD CHEMISTRY

Theoretical aspects of water-holding in meat

(2010) E. Puolanne et al.   MEAT SCIENCE

Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle

(2009) Y.M. Choi et al.   Livestock Science

Role of Calpains in Postmortem Proteolysis in Chicken Muscle

(2008) H. L. Lee et al.   POULTRY SCIENCE