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Studies on the Emulsifying Properties of Some Intracellular Beef Muscle Proteins a b
Author(s) -
HEGARTY G. R.,
BRATZLER L. J.,
PEARSON A. M.
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.tb01671.x
Subject(s) - myosin , sarcoplasm , chemistry , emulsion , myofibril , salt (chemistry) , actin , intracellular , chromatography , biophysics , biochemistry , endoplasmic reticulum , biology , organic chemistry
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.