[Studies of the effect of various freezing processes on myofibrilar proteins of bovine m. longissimus dorsi]
1982
Petrovic, Lj.
Freezing and freezing temperature bring about reduction of ATPase activity. The total solubility rate of myofibrilar proteins of frozen muscles is higher than that of fresh ones, except for those frozen at -20 deg C. Myofibrilar protein content differs in muscle extracts frozen at different temperatures. Viscosity of extracts of 1. muscles frozen at different temperatures is different. Freezing weight loss diminishes with temperature decrease. Free SH groups content in 1. muscles frozen at -78 and -196 deg C is almost identical to that of fresh ones, it is higher in those frozen at -20 deg C and highest in the muscles frozen at -10 deg C. Muscles frozen at -20 deg C are the least and those frozen at -196 deg C the most plastic. Freezing affects the defrosted muscles colour and their1071 total protein content. Cooked frozen muscles are softer than fresh ones. Freesing induces denaturative changes and they are the strongest when freezing at -20 deg C. Denaturating changes of actin take place at all freezing temperatures and those of myosin only at -20 deg C. Changes in the pH value occur in frozen muscles and they are different at different temperatu
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