Suspensions of myosin, actomyosin and sarcoplasmic protein, isolated from beef semitendinosus muscle, were prepared at several protein concentrations and with various amounts of added sodium chloride up to 1.4M. An aliquot from each suspension was pressed between two pieces of muscle of fixed cross‐sectional area and cooked. Binding strength was estimated from the force required to separate the meat pieces. At salt concentrations up to 1M the binding strength of myosin was superior to that of actomyosin (P = 0.05 – 0.001), and that of sarcoplasmic protein was too low to be measured by the techniques that were used. However in the absence of added sodium chloride, a mixture of sarcoplasmic protein and myosin had greatest (P = 0.05) binding strength.

No abstract

No abstract

Suspensions of crude myosin, sarcoplasmic protein and a mixture of both were prepared. Each was mixed with coarsely-ground meat in the ratio 1:lO w/w. The product was formed into frozen rolls, 6.5 cm diameter, from which steakettes 2 cm thick were cut. These were oven broiled to an internal temperature of 70°C and assessed by a laboratory taste panel. The binding strength between meat pieces was also objectively assessed. Overall, taste panel members preferred the products containing added myosin with salt to those without salt or with added sarcoplasmic protein only. Correlations between various attributes of the product were investigated. Significant correlations were found between overall acceptability of the product and flavor, juiciness, tenderness and the objective measurements in binding strength. Significant correlations also were found between the objective and subjective assessments of binding strength.

The feasibility of using myosin, extracted from post-rigor bovine muscle, as a binding agent for meat pieces, was examined. Crude myosin was extracted with solutions containing various concentrations of sodium chloride (salt) and sodium tripolyphosphate (TPP). Maximum yield was obtained using 1M salt and about 0.25% TPP in the extracting solution. Binding strength, i.e. the strength with which pieces of meat adhere, of crude myosin extracted with 1M salt and 0.15, 0.25 or 0.5% TPP were not significantly different and were only slightly lower than that for crude myosin extracted from pre-rigor muscle. The myosin preparations had binding strength much greater than that reported previously for actomyosin. These results show that crude myosin extracted from postrigor bovine muscle has a potential use as a meat binding agent.