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DIFFERENTIAL SCANNING CALORIMETRY CAN DETERMINE KINETICS OF THERMAL DENATURATION OF BEEF MUSCLE PROTEINS
Author(s) -
FINDLAY C. J.,
PARKIN K. L.,
STANLEY D. W.
Publication year - 1986
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1986.tb00085.x
Subject(s) - sarcomere , differential scanning calorimetry , kinetics , tenderness , context (archaeology) , conditioning , chemistry , denaturation (fissile materials) , order of reaction , biophysics , food science , biology , thermodynamics , nuclear chemistry , reaction rate constant , mathematics , endocrinology , myocyte , physics , quantum mechanics , paleontology , statistics
Differential scanning calorimetry (DSC) of beef muscle produced three large endotherms occurring at 55–57°C, 65–67°C and 81–83°C. Based on earlier DSC research on isolated proteins (Privalov 1979), the concept of cooperative units participating in thermal transition phenomena was applied to beef muscle endotherms. Analysis of these endotherms by the van't Hoff relationship and Borchardt and Daniels kinetics analysis revealed reaction orders of ca. 0.6 to 2.1, 3.5 to 5.1 and 1.5 to 3.1, respectively, for the three muscle endotherms. The reaction orders for these endotherms were influenced by muscle type, fiber sarcomere length and conditioning. Aging led to an increase in reaction order whereas increased sarcomere length was accompanied by a decrease in reaction order or number of cooperative units. Changes in the number of cooperative units participating in the endotherms is discussed in the context of meat tenderization and conditioning. It appears reaction order analysis of the T 3 transition (81–83°C) may correlate with meat tenderness.