1Institute of Life Sciences, HES-SO Valais-Wallis, 1950 Sion, Switzerland
Pea protein concentrates (PPCs) contain not only storage proteins but also naturally occurring hydrocolloids such as soluble fibers, pectic polysaccharides, and cell wall fragments, which influence hydration, viscosity, and network formation during high-moisture extrusion. These endogenous hydrocolloids are increasingly recognized as functional co-structuring agents that can enhance or limit the development of fibrous, anisotropic textures in plant-based meat analogues. However, their interactions with proteins are highly sensitive to thermomechanical history and remain poorly characterized under industrially relevant conditions.
This study investigates a sequential thermomechanical processing strategy designed to modulate protein–polysaccharide interactions in commercial PPC and improve its structuring behavior during high-moisture extrusion. In a first step, PPC was subjected to controlled pre-treatment at low moisture (dry-heat conditioning) to adjust solubility, hydration kinetics, and viscoelastic behavior of the native protein–hydrocolloid matrix. This pre-activation step aimed to partially unfold proteins, redistribute water-binding sites, and enhance compatibility with endogenous soluble polysaccharides, thereby improving the functional readiness of the material for subsequent texturization.
In the second step, pre-treated materials were processed under defined high-moisture extrusion conditions. Structural development was evaluated through mechanical anisotropy, macro-texture analysis, and microstructural imaging.
The results demonstrate that sequential processing significantly enhances the structural performance of pea protein systems. Pre-treated samples exhibited higher water-binding capacity and increased viscoelasticity prior to extrusion. During high-moisture texturization, these functional improvements translated into clearer phase alignment, more pronounced fibrillar structures, and increased anisotropy.
Overall, the findings show that tailoring the thermomechanical history of plant protein ingredients can unlock the structuring potential of their intrinsic hydrocolloid components, enabling high-quality meat analogues without the need for purified gums or additives. This approach offers a sustainable, low-energy route for improving texture in plant-based foods while maintaining clean-label formulations and supporting regional protein production