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PRESSURE‐INDUCED SOLUBILIZATION OF MYOFIBRILLAR PROTEINS
Author(s) -
MACFARLANE J. J.,
McKENZIE I. J.
Publication year - 1976
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.1365-2621.1976.tb01191.x
Subject(s) - myofibril , solubilization , chemistry , salt (chemistry) , imidazole , chromatography , muscle protein , electrophoresis , biochemistry , biology , anatomy , organic chemistry , skeletal muscle
In an earlier study it was found that the application of high pressure to homogenates of meat in saline solution could increase water‐holding capacity and promote the solubilization of proteins. These studies have now been extended to myofibrils prepared from sheep semimembrano‐sus muscle. The amount of protein solubilized by pressurization was found to be dependent on (1) temperature, generally being greater at 0°C than at 30°C; (2) the nature and the concentration of the salt; and (3) the pH. SDS gel electrophoresis indicated that solubilization of all the major constituent proteins of the myofibril could be promoted. It is suggested that the imidazole group is implicated in the pressure solubilization effect.