Heat-Induced Gelation of ChickenPectoralis MajorMyosin and β-Lactoglobulin

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Abstract
The denaturation, aggregation, and rheological properties of chicken breast muscle myosin, β-lactoglobulin (β-LG), and mixed myosin/β-LG solutions were studied in 0.6 M NaCl, 0.05 mM sodium phosphate buffer, pH 7.0, during heating. The endotherm of a mixture of myosin and β-LG was identical to that expected if the endotherm of each protein was overlaid on the same axis. The maximum aggregation rate (ARmax) increased, and the temperature at the ARmax (Tmax) and initial aggregation temperature (To) decreased as the concentration of both proteins was increased. The aggregation profile of G‘) when heated to 90 °C and after cooling. β-LG had no effect on the gel point of ≥1.0% myosin, but enhanced gel strength when heated to 90 °C and after cooling. After cooling, the G‘ of 1% myosin/2%β-LG gels was about 1.7 times greater than that of gels prepared from 2% myosin/1% β-LG. Keywords: β-lactoglobulin; myosin; gelation; aggregation; denaturation