High Pressure Processing of Food Proteins

High pressure processing (HPP) is a non-thermal technology that subjects food systems to isostatic pressures typically ranging from 100 to 600 MPa. By perturbing non-covalent bonds within protein molecules, HPP induces partial or complete unfolding, followed by refolding or aggregation on decompression. These structural modifications translate into altered solubility, emulsifying capacity, foaming behaviour, gelling characteristics and digestibility. In plant-based proteins, controlled unfolding can expose hidden hydrophobic patches and sulfhydryl groups, enhancing interactions with enzymes and other food matrix components. In dairy and egg proteins, pressure-induced gel networks exhibit improved textural resilience and water-holding capacity, while in meat and seafood proteins HPP can tenderise muscle fibres and modulate allergenic epitopes. Overall, HPP offers a versatile tool for tailoring techno-functional properties, improving microbial safety and nutritional quality, and facilitating the development of novel protein-rich formulations with minimal impact on flavour and micronutrient retention.

Research from Nature Portfolio

A foundational study examined the structural responses of squid hemocyanin to pressures up to 600 MPa, revealing that high pressure decreases α-helix content and increases random coil structures. Exposure of interior hydrophobic regions and sulfhydryl moieties led to reduced IgE and IgG binding capacities, demonstrating a marked decrease in allergenicity. Detailed modelling of quaternary dissociation under pressure provided mechanistic insight into how conformational shifts can be harnessed to lower seafood allergenicity while preserving the protein’s bioactivity and functional integrity.

High Pressure Processing of Food Proteins publication trend

The graph below shows the total number of articles in high pressure processing of food proteins across all publications each year (not limited to Nature Index journals).

Technical terms

High hydrostatic pressure (HHP): A processing method applying uniform pressure (100–600 MPa) to foods, disrupting non-covalent bonds in proteins without significant heat.

Protein denaturation: The alteration of secondary, tertiary or quaternary protein structures, leading to loss or change of native conformation and function.

Surface hydrophobicity: A measure of the exposure of hydrophobic amino acid residues on the protein surface, influencing emulsifying and foaming behaviour.

Enzymatic hydrolysis: The enzymatic cleavage of peptide bonds, often facilitated by HHP-induced unfolding to release bioactive peptides.

Allergenicity: The potential of a protein to elicit an immune (IgE-mediated) response, which can be reduced by pressure-induced structural alterations.

Emulsifying activity index (EAI): A quantitative measure of a protein’s ability to stabilise oil-in-water emulsions, reflecting interfacial adsorption capacity.

References

1. Effects of high-pressure and transglutaminase, individually and simultaneously applied, on pea and soy protein isolates. Sustainable Food Technology (2023).
2. Structure-based modelling of hemocyanin allergenicity in squid and its response to high hydrostatic pressure. Scientific Reports (2017).
3. Comparative effects of high pressure processing and heat treatment on in vitro digestibility of pea protein and starch. npj Science of Food (2022).
4. High Hydrostatic Pressure: Influences on Allergenicity, Bioactivities, and Structural and Functional Properties of Proteins from Diverse Food Sources. Foods (2024).