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SUMMARY Investigation was made of the effect of pH, enzyme concentration, cysteine, sodium chloride, and temperature on the extent of solubilization of 0.10 N sodium hydroxide‐soluble proteins, elastin, and collagen of biceps femoris muscle of beef by ficin and bromelain. All protein fractions of beef are solu‐biked maximally at pH 7 and 80°C by both ficin and bromelain. Ficin is particularly effective in the solubilization of elastin, even at 20°C. Cysteine and sodium chloride increase the extent of solubilization, especially of collagen and elastin (sodium chloride only). The available data indicate that collagen must be denatured before ficin and bromelain can solubilize it.
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EL‐GHARBAWI et al. (1963) studied this question.
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