LAUSR

BACKGROUND Myosin is the most important component of myofibrillar protein, has excellent gelling properties. So far, heating treatment is still 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 main purpose of this work was to study the effects of different heating rates (1, 2, 3 and 5 °C min-1 ) on the self-assembly 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') and water holding capacity (WHC) compared with higher heating rates (2, 3 and 5 °C min-1 ). At higher temperatures (40 °C, 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, and formed regular and homogeneous spherical aggregates. Therefore, the myosin gel also had a better three-dimensional (3D) 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. This article is protected by copyright. All rights reserved.