Structural and techno-functional modifications of pea protein fractions by non-thermal technologies

Animal-based food production is highly associated with greenhouse gas emissions, land degradation, and animal welfare issues. In response to growing environmental and ethical concerns about this production system, consumers are increasingly adopting more sustainable dietary habits. This shift includes reducing the consumption of animal-derived products in favor of plant-based alternatives, with legumes standing out as a promising source of protein. Pea proteins have gained attention due to their high productivity, low allergenicity, and non-genetically modified (non-GMO) status. Pea is primarily composed of globulins (legumin 11S and vicilin 7S) and albumins 2S, each exhibiting distinct structural and techno-functional properties that influence their behavior in complex food formulations. To overcome formulation challenges, non-thermal technologies (NTTs) such as ultrasound (US), cold plasma (CP), high hydrostatic pressure processing (HPP), and pulsed electric fields (PEF), have emerged as innovative tools for modulating protein structure and improving their techno-functional properties. Despite the promising capacity of NTTs to modify the protein structure and techno-functionalities, the current research remains limited, particularly regarding the impact of these NTTs on isolated protein fractions and their effects in improving plant-based formulations. Consequently, this literature review critically explores the potential of the NTTs to modulate the structure of pea protein fractions, thereby enhancing their techno-functionalities and broadening their utilization in complex food systems.