Protein Gelation and Functional Properties in Food Systems

Protein gelation underpins the texture, stability and sensory qualities of a vast array of food products, from dairy yoghurts and meat analogues to plant-based gels and confectionery. Gelation occurs when soluble proteins unfold and reassociate into a three-dimensional network that immobilises water, entrapping fat droplets and other ingredients. The nature of this network—determined by protein source, concentration, ionic strength, pH and processing conditions—governs key functional properties such as gel strength, elasticity, water-holding capacity and mouthfeel. Enzymatic crosslinking, high-pressure treatments, thermal or cold-set induction and emerging physical methods (ultrasound, ohmic heating) are routinely employed to tailor network architecture. Understanding how molecular interactions translate into macroscopic performance enables the design of lower-fat, cleaner-label and plant-based products without compromising texture or nutrition. Advances in microstructural characterisation and rheological analysis continue to drive innovation in sustainable protein utilisation and novel food formats with controlled digestibility and enhanced consumer appeal.

Research from Nature Portfolio

Recent studies have employed nanoscale imaging and spectroscopy to elucidate the early stages of protein network formation, revealing how modulating ionic bridges and hydrogen bonding can fine-tune gelation pathways. One investigation demonstrated that controlled addition of divalent cations to whey protein solutions directs the assembly of uniform nano-fibrils, resulting in gels with adjustable stiffness and reduced syneresis, suitable for high-protein dairy desserts. Another report showed that targeted enzymatic deamidation of pea protein isolate enhances solubility and promotes the formation of cold-set gels with a homogeneous fibrillar network, markedly improving elasticity and water retention at refrigeration temperatures—an approach that supports low-energy processing of plant-based yoghurts and spreads.

Protein Gelation and Functional Properties in Food Systems publication trend

The graph below shows the total number of articles in protein gelation and functional properties in food systems across all publications each year (not limited to Nature Index journals).

Technical terms

Gelation: The process by which protein molecules unfold and reassemble into a three-dimensional network that traps water and other components, forming a semi-solid structure.

Storage modulus (G’): A rheological parameter quantifying the elastic (energy-storing) behaviour of a gel under oscillatory shear, indicative of network strength.

Water-holding capacity (WHC): The ability of a protein network to retain water against gravitational or mechanical forces, crucial for juiciness and yield.

Deamidation: An enzymatic or chemical modification removing amide groups from protein side-chains, increasing charge density and solubility to influence gel microstructure.

References

1. Effect of High Pressure Homogenization-Modified Soy 11S Globulin on the Gel and Rheological Properties of Pork Myofibrillar Protein. Foods (2023).
2. Effect of ultrasound-assisted sodium bicarbonate treatment on gel characteristics and water migration of reduced-salt pork batters. Ultrasonics Sonochemistry (2022).
3. Physicochemical Characteristics of Protein‐Enriched Restructured Beef Steaks with Phosphates, Transglutaminase, and Elasticised Package Forming. Journal of Food Quality (2018).