High Pressure Processing Effects on Gel Formation in Protein Systems

High pressure processing (HPP) has emerged as a versatile non-thermal technology for modulating the functional properties of proteins and inducing structured gel networks. By subjecting protein suspensions to pressures typically in the range of 100–600 MPa, HPP triggers conformational alterations at secondary, tertiary and quaternary levels. Unfolding of α-helices and exposure of hydrophobic residues promote intermolecular interactions such as hydrophobic clustering, disulfide cross-linking and hydrogen bonding, resulting in three-dimensional networks with enhanced water-holding capacity and tailored texture. The pressure-induced gelation pathways vary with protein origin—myofibrillar proteins from muscle, globular whey or plant proteins—governing gel strength, elasticity and microstructure. Control of pressure magnitude, holding time and temperature enables fine-tuning of rheological parameters, nutrient retention and encapsulation of bioactive compounds. Applications span meat product reformulation, development of emulsion gels for nutrient delivery, reduced-salt gels and novel texturised plant-based matrices. This approach aligns with consumer demand for minimally processed foods and underpins advances in global food sustainability and functional ingredient delivery.

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High Pressure Processing Effects on Gel Formation in Protein Systems publication trend

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Technical terms

High Pressure Processing (HPP): A non-thermal food technology applying uniform hydrostatic pressure (typically 100–600 MPa) to modify molecular structures and functional properties without significant heating.

Myofibrillar Protein: Muscle-derived proteins (e.g. myosin and actin) responsible for gel formation and texture in meat products under pressure or heat treatment.

Gelation: The transition of a dispersed protein solution to a semi-solid network through intermolecular interactions, trapping water within a three-dimensional matrix.

Elastic Modulus (G’): A measure of the stored energy and solid-like behaviour in a gel, indicating its stiffness under oscillatory deformation.

Viscous Modulus (G”): A measure of the dissipated energy and liquid-like behaviour in a gel, reflecting its flow resistance under oscillatory stress.

Secondary Structure: Localised protein folding motifs such as α-helices and β-sheets that are altered under pressure to drive network formation.

References

1. Ultra-high pressure improved gelation and digestive properties of Tai Lake whitebait myofibrillar protein. Food Chemistry X (2023).
2. Preparation, Characterization and Formation Mechanism of High Pressure-Induced Whey Protein Isolate/κ-Carrageenan Composite Emulsion Gel Loaded with Curcumin. Gels (2024).
3. Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review. Foods (2021).