Bovine Muscle Tenderness as Related to Protein Solubility

The longissimus (modest degree of marbling) from forty beef ribs selected 48–56 hr post‐mortem was used in two trials. Trial I involved A, C and E maturity ribs (10 each classification). Each rib was subjectively scored for texture (fresh) and adjacent longissimus samples were removed for the determination of protein solubility (fresh) and tenderness. Tenderness (cooked muscle) was measured with a Warner‐Bratzler shear and taste panel. Protein solubilities were determined using 0.154M Krebs‐Ringer‐Bicarbonate buffer, 0.2M KCl + 0.01M K phosphate buffer, 1.1M Kl + 0.1M K phosphate buffer, and 0.03M K phosphate buffer. Trial II involved 10 A maturity ribs. The 0.2M KCl, 1.1M Kl and 0.03M K phosphate buffers as described for trial I were used for protein extraction. Additionally, sarcomere length was measured in formalin. Multiple regression equations were developed to predict tenderness in trial II. Protein solubilities were not significantly different between the carcass maturity groups although there were trends toward increased solubility as maturity increased. Tenderness tended to decrease from A to E maturity indicating a negative relationship between protein solubility and tenderness. Several significant negative correlations between protein solubility and tenderness were found in trial I (A maturity group) and trial II. Additionally, several significant negative correlations between texture and solubility were calculated. Correlations within the C and E maturity groups were variable and showed no definite trends. Multiple regression analyses showed that a combination of protein solubilities, texture score and sarcomere length accounted for 88% of the variation in shear force and 72% of the variation in taste panel tenderness.