Conditions leading to the development of warmed-over flavor in uncured cooked meat were studied. Beef muscle which had been thoroughly extracted with water did not develop warmed-over flavor indicating that the substance responsible for initiating the reaction was water soluble. A water extract from muscle tissue was fractionated by dialysis and column chromatography, and the various fractions were added back to water-extracted tissue. The development of warmed-over flavor in this system was followed by TBA analysis and odor evaluation. Heme compounds ware found to have little effect on the development of warmed-over flavor in this system. The reaction was apparently catalyzed by ferrous iron and ascorbate. It is considered that ascorbic acid functions by keeping at least a portion of the iron in the ferrous state. At higher levels ascorbic acid inhibited the reaction, possibly by upsetting a balance between ferrous and ferric iron.

SUMMARY The emulsifying capacity curves for actin, myosin, actomyosin, and sarcoplasmic proteins were determined under various conditions. The proteins were ranked from greatest emulsifying capacity to least as follows: actin in the absence of salt, myosin, actomyosin, sarcoplasmic proteins (water extracted), and actin in 0.3M salt. Myosin and actomyosin produced emulsions with superior stability; however, at the pH of normal fresh meat (5.6–5.8), the sarcoplasmic fraction produced the most stable emulsions. Actin produced very stable emulsions under all conditions. The amount of protein utilized in the formation of an interface appeared to be related to the stability of au emulsion. NPN compounds were found to have no role in emulsion formation.

No abstract

SUMMARY A procedure developed to fractionate the major nitrogen‐containing components of muscle was utilized to study the relationship of intracellular muscle proteins to tenderness. The study was performed on a group of 20 yearling bulls from two lines of cattle that had been selected for differences in tenderness. The longissimus dorsi muscle contained more total nitrogen per unit of muscle tissue and almost twice as much sarcoplasmic protein as the infra‐spinatus muscle. The longissimus dorsi contained less fibrillar protein and non‐protein nitrogen than the infraspinatus. The following factors were correlated with tenderness as measured by shear and panel: sarcoplasmic protein nitrogen/total fibrillar protein nitrogen; soluble fibrillar protein nitrogen/ total fibrillar protein nitrogen; water released/total water. Fibrillar protein solubility was highly correlated with tenderness (r.=−0.69 for shear and r= 0.59 for panel). An r value of 0.49, significant at the 5% level, was found between water‐holding capacity and tenderness as measured by the shear.

SUMMARY– The formation of a calcium polyphosphate precipitate in curing pickles is dependent upon brine strength, brine temperature, tripolyphosphate concentration and calcium concentration. The highest concentration of calcium at which no precipitate is formed under various conditions is referred to as the critical calcium concentration. A series of curves is presented from which the critical calcium concentration can be determined for any practical combination in solution of NaCl, sodium tripolyphosphate and calcium ions. The effect on the critical calcium concentration of temperature, pH and added sucrose was also determined and graphically presented. In some cases, added CaSO4 caused a significant increase in the water holding capacity of cured ground ham, and in no instance did the calcium salt cause a reduction in water‐holding capacity. The yield of fully‐cooked cured hams was not affected by curing with phosphate pickles containing abnormally high levels of CaSO4.