Abstract
Themechanismofheatinducedmuscleproteingelationhasbeensubjectedto extensive studies.Thepresentpaper reviews the latest literature concerning unfolding, aggregation and gelation of poultry muscle myofibrillar proteins with respect to muscle type, pH and heating conditions. It is stressed that under dynamic conditions aggregation plays a major role in producing gel elasticity differences between white and red myofibrillar proteins. Heat-induced chicken breast myosin gelation proceeds with unfolding of LMM, S-1subfragment and alkali LC followed by aggregation (LMM, S-1) and matrix formation. It is hoped that the present review will encourage further research and stimulate discussion to explaingelationmechanism of poultry as wellas mammalian muscle proteins, e.g., rheological transitions withinthe 50^60C temp. range.
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