The influence of cooling die temperature gradients on the texture of high-moisture meat analogs

Abstract

In this study, we used protein blends and rheological methods to simulate the structural changes in high-moisture meat analogs (HMMA) within the cooling die and clarified the complex interactions between changes in protein composition and HMMA's textural characteristics. Rheological analysis revealed a decrease in rheological parameters with an increase in the cooling die temperature, although no structural collapse was observed in gel stability. Although the hardness of HMMA decreased with an increase in the cooling die temperature, it facilitated the alignment of protein structures, resulting in an enhanced texturization index. Notably, this temperature increase led to a reduction in β-sheets and α-helix structures, which typically contributed to the stiffness and cohesion of protein networks, whereas β-turns increased, affecting the flexibility of proteins. Among the various chemical interactions, disulfide bonding uniquely increased at high temperatures, underscoring its critical role in the formation of fibrous structures.

Keywords: High-moisture extrusion; Protein gel; Protein network; Rheological approach; Temperature fraction cooling die.