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Influence of Temperature, Time and Solvent on the Solubility of Corium Collagen and Meat Proteins
Author(s) -
KENNEY P. B.,
HENRICKSON R. L.,
CLAYPOOL P. L.,
RAO B. R.
Publication year - 1986
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.1365-2621.1986.tb11108.x
Subject(s) - chemistry , solubility , salt (chemistry) , dilution , solubilization , solvent , nitrogen , food science , sodium , chromatography , extrusion , biochemistry , organic chemistry , materials science , physics , metallurgy , thermodynamics
Collagen replacement (0, 10, 20, 30, or 100%) of minced muscle reduced the quantity of salt (NaCl) soluble nitrogen in unheated samples. This dilution of salt soluble meat protein with salt insoluble collagen was evident at each time period (0, 15, 30, 45, 60, 75, or 90 min) of heating. When sufficient heat was applied (i.e. high temperature for prolonged period), the solubilization of the collagen component of the meat block negated the difference in soluble nitrogen associated with collagen replacement. The presence of sodium tripolyphosphate (STPP) appeared to suppress the solubilization of collagen as a result of the initial high pH but enhanced the solubilization of minced muscle.