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Factors Affecting Enzymatic Solubilization of Beef Proteins
Author(s) -
ELGHARBAWI M.,
WHITAKER J. R.
Publication year - 1963
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1963.tb00177.x
Subject(s) - chemistry , elastin , solubilization , sodium , sodium hydroxide , bromelain , chromatography , biochemistry , enzyme , organic chemistry , papain , biology , genetics
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.