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Thermal Transitions of Salt‐soluble Proteins from Pre‐ and Postrigor Chicken Muscles
Author(s) -
XIONG Y.L.,
BREKKE C.J.
Publication year - 1990
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.1365-2621.1990.tb03563.x
Subject(s) - differential scanning calorimetry , denaturation (fissile materials) , chemistry , salt (chemistry) , chicken breast , calorimetry , biochemistry , biophysics , food science , biology , nuclear chemistry , thermodynamics , organic chemistry , physics
Salt‐soluble protein (SSP) was extracted from pre‐ and postrigor chicken muscles at various pH values, and protein thermal denaturation was studied using several techniques. Heating at 1°C/min from 20 to 70°C induced a three‐ to fourfold increase in breast and leg hydrophobicity. Differential scanning calorimetry of breast and leg SSP showed a major transition occurring within the range 55 to 64°C, with the value dependent on rigor state and pH. Protein‐protein association, as measured by turbidity change upon heating, underwent two transitions for leg SSP and two or three for breast SSP. The specific transition temperature and rate were dependent on pH, muscle type and rigor state. However, muscle type and pH had a greater effect than muscle rigor state on SSP denaturation.