Understanding mechanisms of myofibrillar protein gelation is important for development of gel-type muscle foods. The protein-protein interactions are largely responsible for the heat-induced gelation. Exogenous additives have been extensively applied to improve gelling properties of myofibrillar proteins. Research has been carried out to investigate effects of different additives on protein gelation, among which low molecular substances as one of the most abundant additives have been recently implicated in the modifications of intermolecular interactions. In this review, the processes of myosin dissociation under salt and the subsequent interaction via intermolecular forces are elaborated. The underlying mechanisms focusing on the role of low molecular additives in myofibrillar protein interactions during gelation particularly in relation to modifications of the intermolecular forces are comprehensively discussed, and six different additives i.e. metal ions, phosphates, amino acids, hydrolysates, phenols and edible oils are involved. The promoting effect of low molecular additives on protein interactions is highly attributed to the strengthened hydrophobic interactions providing explanations for improved gelation. Other intermolecular forces i.e. covalent bonds, ionic and hydrogen bonds could also be influenced depending on varieties of additives. This review can hopefully be used as a reference for the development of gel-type muscle foods in the future.
Keywords: Intermolecular forces; low molecular substances; myosin dissociation; myosin interactions; protein conformation.