Abstract
ABSTRACTThe present study was designed to analyze the formation mechanics of heat-induced myofibrillar gels from rabbit psoas major at 0.6 mol/L KCl (pH 6.5) and 0.2 mol/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°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.
Highlights
Gel-forming ability is one of the most important functional properties of meat proteins in which myofibrillar proteins play the most important role
Sharp and Offer (1992) investigated the gathering manner of rabbit skeletal myosin molecules after heating at 30–60°C for 30 min using transmission electron microscopy (TEM), and they believed that the head–head interactions, head–tail interactions and tail–tail interactions were the basic mechanics of gelation
The myofibrils prepared at different temperatures and ionic strengths were observed using phase-contrast microscopy, and the microstructural changes are shown above
Summary
Gel-forming ability is one of the most important functional properties of meat proteins in which myofibrillar proteins play the most important role. The mechanics of heat-induced gelation of myofibrillar proteins has been studied for more than half a century. Hermansson, Harbitz, and Langton (1986) investigated the gelation of myosin treated at different pH and ionic strengths and found different gel structures. The heat-induced gelation was associated with the formation of sufficient intermolecular protein bonds such as hydrogen bonds, ionic linkages, hydrophobic interactions and covalent bonds (Lanier, Yongsawatdigul, & CarvajalRondanelli, 2013). The formation of heat-induced gels is a complex thermodynamic process that is related to the muscle sources and types and different cooking conditions such as temperature, pH, protein concentrations and ionic strength (Lanier et al, 2013) and most of the researches focused on the study of myosin heat-induced gelation
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