Background: The properties of pea protein isolate (PPI), comprising a sustainable plant-derived protein for which the full functional potential in complex food matrices remains unrealized as a result of inherent limitations in food applications, are investigated in this work under gamma (γ) irradiation (0-10 kGy). The study used non-thermal physical treatment, namely γ irradiation, using ionizing radiation from a 60Co source, which causes controlled structural rearrangements in macromolecules.
Results: Fourier transform infrared spectroscopy deconvolution revealed irradiation-induced changes: partial unfolding of secondary structures (α-helix/β-sheet), whereas scanning electron microscopy showed fragmented morphology (4-8 kGy) and aggregated clusters. Functional properties peaked at 8 kGy with solubility, emulsifying activity and water/oil-holding capacity, whereas 10 kGy enhanced emulsion stability but reduced solubility because of disulfide cross-linking.
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