Effects of heating rates on the self‐assembly behavior and gelling properties of beef myosin

Abstract

BACKGROUND: Myosin is the most important component of myofibrillar protein, with excellent gelling properties. To date, heating treatment remains the mainstream method for forming gel in meat products, and it has the most extensive application in the field of meat industry. However, at present, there are few reports on the effects of heating rates on myosin self-assembly and aggregation behavior during heating treatment.RESULTS: The present study aimed to investigate the effects of different heating rates (1, 2, 3 and 5 °C min −1 ) on the selfassembly behavior, physicochemical, structural and gelling properties of myosin. At the lowest heating rate of 1 °C min −1 , the myosin gel had a dense microstructure, the highest elastic modulus (G 0 ) and water holding capacity compared to higher heating rates (2, 3 and 5 °C min −1 ). At higher temperatures (40, 45 °C), the surface hydrophobicity, turbidity, particle size distribution and self-assembly behavior of myosin in pre-gelling solutions showed that myosin had sufficient time to denature, underwent full structure unfolding before aggregation at the heating rate of 1°C min −1 , and formed regular and homogeneous spherical aggregates. Therefore, the myosin gel also had a better three-dimensional network.CONCLUSION: The heating rates had an important effect on the quality of myosin gels, and had theoretical implications for improving the quality of meat gel products.

Regulation of Protein Flexibility and Promoting the Cod Protein Gel Formation Using Ultrasound Treatment

“…Under appropriate conditions, like heating, and a pH level of 7.0, proteins have the ability to undergo self-assembly processes resulting in the formation of crystals, aggregates, and gels. Despite their distinct final forms, these self-assembly aggregates are all generated through protein–protein interactions that are influenced by comparable thermodynamic parameters . Fang et al claimed that the structure of myosin, the main constituent of muscle proteins, unfolding and hydrophobic groups exposed are the trigger conditions for self-assembly.…”

“…Despite their distinct final forms, these self-assembly aggregates are all generated through protein–protein interactions that are influenced by comparable thermodynamic parameters . Fang et al claimed that the structure of myosin, the main constituent of muscle proteins, unfolding and hydrophobic groups exposed are the trigger conditions for self-assembly. The self-assembly of supramolecular hydrogels is driven by noncovalent interactions, resulting in the formation of fibrils that bundle into fibers and entangle to create a three-dimensional (3D) network .…”

“…Under appropriate conditions, like heating, and a pH level of 7.0, proteins have the ability to undergo self-assembly processes resulting in the formation of crystals, aggregates, and gels. Despite their distinct final forms, these self-assembly aggregates are all generated through protein–protein interactions that are influenced by comparable thermodynamic parameters .…”