Mechanism of rheological changes in poultry myofibrillar proteins during gelation

The mechanism of heat induced muscle protein gelation has been subjected to extensive studies. The present paper 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-1 subfragment 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 explain gelation mechanism of poultry as well as mammalian muscle proteins, e.g., rheological transitions within the 50-60 degreesC temp. range.