The mechanics of formation of heat-induced myofibrillar protein gel from rabbit psoas major

The present study was designed to analyze the formation mechanics of heat-induced myofibrillar gels from rabbit psoas major at 0.6mol/L KCl (pH 6.5) and 0.2mol/L KCl (pH 6.0; n=3). Morphological structure changes were observed using phase-contrast microscopy, transmission electron microscopy, scanning electron microscopy (SEM) and gel properties were determined through water-holding capacity (WHC), gel strength and dynamic rheological test. The results revealed that myofibrillar filaments aggregated and formed larger oligomers by side-by-side interactions when heated from 25 to 65 degrees C. In higher ionic strength at higher pH, the filaments formed a more compact homogeneous network structure and the G value was much lower with higher WHC and gel strength, suggesting that the myofibril gel properties could be described by G. Based on the present study, it is suggested that the desired structural and textural attributes of myofibril gel can be manipulated by temperature, ionic strength and pH.