ABSTRACT
The lean portion of meat contains roughly 20% protein, with only slight variations in the content between different species. In addition to their high content in muscle tissues, the muscle proteins are valued for their high nutritional quality and superior functional performance. Traditionally, the proteins found in muscle have been classified into categories according to their distribution, organization, solubility, and function in the living muscle tissue. However, the quality of comminuted or restructured meat products is dependent on the functionality of the protein matrix within the products. An alternative approach is to apply the quantitative structure-activity relationship to predict functionality of the ingredients from basic properties of the proteins, including properties such as charge, surface hydrophobicity, and solubility. The changes in surface hydrophobicity of salt-extractable proteins as a function of different postmortem storage times at above-freezing temperature were monitored for beef neck muscle and chicken breast muscle.
