Gelation Processes in Protein-Based Hydrogels

Protein-based hydrogels are three-dimensional, water-swollen networks formed through the self-assembly or chemically induced association of protein molecules. Gelation processes rely on a range of molecular interactions—hydrophobic forces, hydrogen bonding, electrostatic attraction and disulfide bridging—to stabilise network structures. Trigger mechanisms include thermal denaturation, pH adjustment, enzymatic action and the addition of multivalent ions or small-molecule cross-linkers. As proteins unfold, reactive sites become exposed, allowing controlled association and network formation. The mechanical properties of the resulting hydrogel—elasticity, viscosity, porosity and water-holding capacity—can be finely tuned by adjusting protein concentration, ionic strength, temperature profile and processing sequence. Owing to their biocompatibility, biodegradability and tunable architecture, protein hydrogels find widespread application in food structuring, controlled release systems, tissue engineering scaffolds and wound-healing dressings. Recent efforts have also explored hybrid systems combining proteins with polysaccharides or synthetic polymers, offering enhanced stability and novel functional attributes. The convergence of advanced rheological characterisation, microstructural imaging and molecular spectroscopy continues to deepen understanding of gelation kinetics and network evolution, paving the way for precision design of protein-based hydrogel materials.

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Gelation Processes in Protein-Based Hydrogels publication trend

The graph below shows the total number of articles in gelation processes in protein-based hydrogels across all publications each year (not limited to Nature Index journals).

Technical terms

Gelation: The transition of a protein solution into a semi-solid network through molecular association and cross-link formation.

Hydrogel: A polymeric network, often protein-based, that retains a large fraction of water within its interstitial spaces.

Cross-linking: The creation of covalent or non-covalent bonds between protein chains, stabilising the three-dimensional gel network.

Rheological properties: The flow and deformation characteristics of a gel, including measurements of elasticity (storage modulus) and viscosity (loss modulus).

References

1. Investigating Texture and Freeze–Thaw Stability of Cold-Set Gel Prepared by Soy Protein Isolate and Carrageenan Compounding. Gels (2024).
2. Binary Alginate-Whey Protein Hydrogels for Antioxidant Encapsulation. Antioxidants (2023).
3. Effect and Mechanism of Acid-Induced Soy Protein Isolate Gels as Influenced by Cellulose Nanocrystals and Microcrystalline Cellulose. Foods (2022).