Gelation Mechanisms in Plant-Based Protein Systems
Summary
Plant proteins form gels through a variety of mechanisms driven by changes in pH, temperature, enzyme activity and ionic environment. Heat treatment unfolds globular proteins, exposing hydrophobic patches and reactive side chains that associate via hydrophobic interactions and disulfide bonds to create a three-dimensional network. Acid-induced gelation relies on gradual protonation, often achieved with glucono-δ-lactone, which lowers the net charge of protein molecules and promotes aggregation through attractive electrostatic forces. Enzymatic crosslinking, most commonly via microbial transglutaminase, links glutamine and lysine residues to reinforce network integrity, modulating gel strength, water-holding capacity and digestibility. In mixed systems, complementary and antagonistic interactions arise: some binary blends exhibit linear mixing behaviour where gel properties scale with composition, while others display synergistic or weakening effects due to mismatched aggregation kinetics or steric hindrance. Control of pre-treatment conditions such as preheating temperature and duration further tailors the microstructure, yielding networks with variable pore size, viscoelasticity and functional performance. These gelation strategies underpin a range of applications in meat analogues, dairy alternatives, plant-based yoghurts and encapsulation matrices, contributing to sustainable protein innovation and novel textural experiences for consumers.
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Gelation Mechanisms in Plant-Based Protein Systems publication trend
The graph below shows the total number of articles in gelation mechanisms in plant-based protein systems across all publications each year (not limited to Nature Index journals).
Technical terms
Gelation: The transformation of a liquid protein dispersion into a semi-solid network through intermolecular associations.
Glucono-δ-lactone (GDL): A slowly hydrolysing acidifier used to lower pH uniformly, triggering acid-induced protein aggregation.
Transglutaminase: An enzyme that catalyses covalent crosslinks between glutamine and lysine residues, strengthening protein networks.
Viscoelasticity: The combined viscous and elastic response of a material under deformation, reflecting both flow and recovery behaviour.
Preheating: A thermal pretreatment applied to protein dispersions to alter conformation, solubility and aggregation propensity before gelation.
References
- Mixing plant-based proteins: Gel properties of hemp, pea, lentil proteins and their binary mixtures. Food Research International (2022).
- Effect of Transglutaminase Pre-Crosslinking Treatment Incorporated with Glucono-δ-lactone on the Physicochemical and Digestive Properties of Tofu. Polymers (2022).
- Acid-induced gels from mixtures of micellar casein and pea protein: Effect of protein ratio and preheating route. Food Hydrocolloids (2024).
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