# Gelling Characteristics and Mechanisms of Heat-Triggered Soy Protein Isolated Gels Incorporating Curdlan with Different Helical Conformations

## TL;DR

This study shows how curdlan with a triple-helix structure improves the gelling properties of soy protein isolate when heated.

## Contribution

The novel contribution is identifying that triple-helix curdlan enhances soy protein gel properties more effectively than other helical forms.

## Key findings

- Triple-helix curdlan significantly improves gel strength, water-holding capacity, and thermal stability of soy protein gels.
- The triple-helix structure promotes a denser and more uniform microstructure in the composite gels.
- Stronger hydrogen bonding between triple-helix curdlan and soy proteins enhances network formation.

## Abstract

This study investigated the effects of curdlan (CUR) with different helical conformations on the gelling behavior and mechanisms of heat-induced soy protein isolate (SPI) gels. The results demonstrated that CUR significantly improved the functional properties of SPI gels, including water-holding capacity (0.31–5.06% increase), gel strength (7.01–240.51% enhancement), textural properties, viscoelasticity, and thermal stability. The incorporation of CUR facilitated the unfolding and cross-linking of SPI molecules, leading to enhanced network formation. Notably, SPI composite gels containing CUR with an ordered triple-helix bundled structure exhibited superior gelling performance compared to other helical conformations, characterized by a more compact and uniform microstructure. This improvement was attributed to stronger hydrogen bonding interactions between the triple-helix CUR and SPI molecules. Furthermore, the entanglement of triple-helix CUR with SPI promoted the formation of a denser and more homogeneous interpenetrating polymer network. These findings indicate that triple-helix CUR is highly effective in optimizing the gelling characteristics of heat-induced SPI gels. This study provides new insights into the structure–function relationship of CUR in SPI-based gel systems, offering potential strategies for designing high-performance protein–polysaccharide composite gels. The findings establish a theoretical foundation for applications in the food industry.