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<p>The impacts of pulsed electric fields (PEF) at 10&#xa0;kV/cm with pre-heating (35–45&#xa0;°C for 22&#xa0;s) on protein structure and functionality were investigated in oat-pea protein blended milk alternatives (OPMA). Protein structural analysis of PEF-treated OPMA revealed substantial tertiary rearrangements, leading to the exposure of hydrophobic (e.g., tryptophan and tyrosine) and charged residues, as well as the potential formation of protein–nonprotein aggregates. As the specific energy increased (81–215&#xa0;kJ/L), a strong correlation (<i>r</i> &gt; 0.8) was observed between the reduction in the median particle sizes of OPMA (by up to 91%) and the enhanced solubility of globular pea proteins (vicilin and legumin). The acid-induced gelation properties of PEF-treated OPMA improved concurrently, facilitating the formation of semi-solid textures during subsequent fermentation. These findings highlight PEF as a potential protein modification tool while providing novel insights into its effects in complex plant protein-rich systems.</p> Graphical Abstract <p></p>

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Pulsed Electric Field Processing Modifies Protein and Nonprotein Components in a Blended Oat-Pea Model Milk and Yoghurt Alternative: Molecular Insights and Impacts on Key Functionalities

  • 期刊论文

  • 发表日期：

    2025年10月25日

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  • Nicholas Horlacher,
  • Jervee M. Punzalan,
  • Jessie King,
  • Sze Ying Leong,
  • Dominic Agyei,
  • Keith C. Gordon,
  • Gert-Jan Moggré,
  • Kevin Sutton,
  • Indrawati Oey

摘要

The impacts of pulsed electric fields (PEF) at 10 kV/cm with pre-heating (35–45 °C for 22 s) on protein structure and functionality were investigated in oat-pea protein blended milk alternatives (OPMA). Protein structural analysis of PEF-treated OPMA revealed substantial tertiary rearrangements, leading to the exposure of hydrophobic (e.g., tryptophan and tyrosine) and charged residues, as well as the potential formation of protein–nonprotein aggregates. As the specific energy increased (81–215 kJ/L), a strong correlation (r > 0.8) was observed between the reduction in the median particle sizes of OPMA (by up to 91%) and the enhanced solubility of globular pea proteins (vicilin and legumin). The acid-induced gelation properties of PEF-treated OPMA improved concurrently, facilitating the formation of semi-solid textures during subsequent fermentation. These findings highlight PEF as a potential protein modification tool while providing novel insights into its effects in complex plant protein-rich systems.

Graphical Abstract