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RELATIONSHIPS BETWEEN BINDING QUALITY OF MEAT AND MYOFIBRILLAR PROTEINS: III: Contribution of Myosin A and Actin to Rheological Properties of Heated Minced‐Meat Gel
Author(s) -
NAKAYAMA TERUO,
SATO YASUSHI
Publication year - 1971
Publication title -
journal of texture studies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.593
H-Index - 54
eISSN - 1745-4603
pISSN - 0022-4901
DOI - 10.1111/j.1745-4603.1971.tb00274.x
Subject(s) - myosin , rheology , pyrophosphate , myofibril , chemistry , myosin head , elasticity (physics) , actin , biophysics , food science , materials science , biochemistry , myosin light chain kinase , enzyme , composite material , biology
Myosin A and myosin B gels formed by heating exhibited similar binding abilities as measured by the breaking energy, but different physical properties. At equivalent concentrations, myosin A gels exhibited smaller values for the Young's modulus of elasticity and larger values for strain at the breaking point. It was inferred from the results of a simple model experiment that in sausage manufacture the physical properties of the heat set minced meat gel are of the myosin B type when no pyrophosphate is present, and similar to the myosin A type when pyrophosphate is added. In the latter case, the contribution of actin may be significant. The binding quality of the heat set myosin B gel increased with myosin concentration. Hence, the binding quality of sausage should be influenced by the myosin B content of meat.