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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-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 explain gelation mechanism of poultry as well as mammalian muscle proteins, e.g., rheological transitions within the 50^60 C temp. range.

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The objective of this study was to improve the rheological (storage modulus G'; phase angle δ) and textural (hardness; breaking force) properties of nitrite-cured sausage batters prepared from pale, soft, exudative (PSE) pork with microbial transglutaminase (TG) using isolated myofibrillar protein (MP) or MP extracted by sodium tripolyphosphate (TPP) as substrates. While TG alone significantly enhanced G', δ and hardness, its combination with TPP was more pronounced as these product quality parameters were increased to the level equal to that of the counterpart batter made from normal (red, firm, non-exudative, RFN) pork. The addition of MP had negligible such effect on TG functions. Cooking loss of TG-treated RFN and PSE meat with TPP was minimal but the batters were less bright (L*) than other treatments. Redness (a*) was variable between treatments. Therefore, texture-related properties of comminuted PSE meat products can be restored to the RFN level by TG cross-linking of protein that is extracted by TPP.