ArticleGels (Basel, Switzerland)2026
High-Temperature Gelation and Structural Characterisation of Commercial Yellow Pea, Faba Bean, and Mungbean Protein-Starch Systems.
Article in Gels (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Heat-Induced Gelation of Legume Protein-Starch Systems: Mechanisms, Structure-Function Relationships and Food Application.Gels (Basel, Switzerland) · 2026Review
- Article
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Authors and funding
4 authors.
Funding
Abstract
The heating of plant proteins at high temperatures is often associated with phase separation due to the aggregation of protein fractions, resulting in weak or discontinuous gels in liquid processing systems. This study examined the high-temperature gelation behaviour of commercial yellow pea, faba bean, and mungbean protein isolates and evaluated how different levels of dry-fractionated starch substitution tailor viscosity development and final gel strength. To characterise structural changes during heating, pasting behaviour was evaluated at 95 °C and 120 °C using a high-temperature Rapid Visco Analyser, while gel strength, temperature-ramp rheology, and thermal transitions were measured using a texture analyser, rheometer, and Differential Scanning Calorimetry. At 95 °C, all systems showed controlled pasting behaviour, with yellow pea exhibiting moderate viscosity development and clear recovery during cooling, mungbean generating the highest peak viscosity, and faba bean forming the strongest elastic network and gel structure. At 120 °C, yellow pea showed reduced stability, whereas faba bean and mungbean retained higher viscosity during heating. Starch addition improved the viscosity stability and gel strength across all proteins by limiting excessive aggregation and supporting network formation. These findings clarify how protein type and starch substitution affect high-temperature gelation, supporting the development of a heat-stable, clean-label plant-based gel system.
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