Thermally Induced Interactions and Gelation of Combined Myofibrillar Protein from White and Red Broiler Muscles

Abstract

The gelling properties of broiler myofibrillar protein were studied by determining protein-protein interactions during heating. Breast and leg salt-soluble protein (SSP) showed l-3 transitions in protein-protein interactions within pH 5.5-6.5. The maximum transition temperatures of leg SSP decreased when leg SSP was mixed with breast SSP. The combined breastileg myofibrils formed stronger gels than leg myofibrils alone at pH B 6.0, and stronger gels than breast myofibrils alone at pH < 6.0. The results suggest that interactions existed between breast and leg myofibrillar proteins, and the transitions in these interactions were useful for predicting gel strength of the combined breast/ leg myofibrils.

Heat‐Induced Gelation of Myofibrillar Proteins and Myosin from Fast‐ and Slow‐Twitch Rabbit Muscles

“…The lower gelling ability of SMp proteins than of those from PM muscle confirmed reports on poultry (Asghar et al, 1984;Morita et al, 1987;Xiong, 1992) and bovine (Fretheim et al, 1986;Egelandsdal et al, 1995) proteins. Except for the myofibrils, the fast muscle type had a greater effect on rigidity at 80ЊC, increasing twofold with pure myosin and fourfold with myosin with C-protein than on the peak rigidity at lower temperatures (Table 2).…”

Effect of single-cycle and multiple-cycle high-pressure treatments on the colour and texture of chicken breast fillets

“…Information on the effect of HP processing on chicken breast meat is scarce, although the effect of heat on chicken white muscle proteins has been reported. Molecular changes in chicken proteins induced by heating follow the sequence molecular unfolding, molecular association, and gel network formation (Xiong, 1992). When ground chicken breast patties were heated at 80°C in a water Table 1 Colour parameters of chicken breast fillets before and after high-pressure processing at 400 MPa (initial processing temperature, 5°C) by single-cycle and multiple-cycle treatments.…”

Gelation of Crude Myofibrillar Protein Isolated From Beef Heart Under Antioxidative Conditions

“…The pellets were stored at 2°C for 16-18 hr before heating to form gels. Protein gels were prepared in 16.5 mm (diameter) x 100 mm (length) glass vials by heating from 20 to 65°C at 0.75Vmin as described (Xiong, 1992).…”