Heat-induced gelation of chicken Pectoralis major myosin and beta-lactoglobulin

The denaturation, aggregation, and theological properties of chicken breast muscle myosin, beta -lactoglobulin (beta -LG), and mixed myosin/beta -LG s olutions 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 beta -LG was id entical to that expected if the endotherm of each protein was, overlaid on the same axis. The maximum aggregation rate (AR(max)) increased, and the te mperature at the AR(max) (T-max) and initial aggregation temperature (T-0) decreased as the concentration of both proteins was increased. The aggregat ion profile of <0.5% myosin was altered by the presence of 0.25% beta -LG. Addition of 0.5-3.0% beta -LG decreased storage moduli of 1% myosin between 55 and 75 degreesC, but increased storage moduli (G ') when heated,to 90 d egreesC and after cooling. beta -LG had no effect on the gel point of great er than or equal to1.0% myosin, but enhanced gel strength when heated to 90 degreesC and after cooling. After cooling, the G ' of 1% myosin/2%beta -LG gels was about 1.7 times greaterthan that of gels prepared from 2% myosin/ 1% beta -LG.