Heat – Induced Gelation and Rheology of Pulse Protein: Implications of Dry and Wet extraction

Dry fractionation for protein extraction has been emerging as an environmentally sustainable alternative to traditional wet extraction method, preserving the native structure and functionality of pulse proteins. However, protein functionality such as gelation in dry fractionated protein concentrate differs compared to wet extracted isolate, primarily due to the presence of excessive non – protein macromolecules. While the gel formation mechanisms of plant proteins and polysaccharides are well established, the gel microstructures of protein as the dominant phase – starch composite gels, particularly for dry fractionated pulse proteins are overlooked. This review provides a comprehensive articulation on the storage protein profiles and molecular structures in dry fractionated pulse protein concentrates, followed by a critical insight into heat – induced gelation mechanisms and microstructure, and rheological modelling. As the rheological models and their application vary depending on the gel formation mechanisms governed by the composition and structure of biopolymers, further research is necessary to describe the complex dry fractionated protein gel networks and their inter relationships with rheological attributes, in conjunction with advanced microscopic and scattering techniques. • Dry-fractionated pulse protein concentrates are more sustainable and retain native functionality but have lower protein purity than wet isolates. • Gel properties depend on the dominant seed storage proteins. • Dry-fractionated concentrates and wet-extracted isolates show distinct rheological behaviours. • Heat-induced gelation mechanisms vary with biopolymer type and microstructure. • Rheological models quantify gel point, flow behaviour, viscoelasticity, microstructure, and time-dependent responses.