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BINDING OF MEAT PIECES: A COMPARISON OF MYOSIN, ACTOMYOSIN AND SARCOPLASMIC PROTEINS AS BINDING AGENTS
Author(s) -
MACFARLANE J. J.,
SCHMIDT G. R.,
TURNER R. H.
Publication year - 1977
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.1365-2621.1977.tb08437.x
Subject(s) - sarcoplasm , myosin , chemistry , sodium , biophysics , biochemistry , salt (chemistry) , endoplasmic reticulum , biology , organic chemistry
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.