<p>This study investigates how Maillard-induced structural reorganization of pumpkin seed protein isolate (PSP) conjugated with different types of polysaccharides, pectin (WP), gum arabic (WG), and sodium alginate (WS) governs emulsion functionality and oxidative stability. Conjugates synthesized via wet heating exhibited advanced glycation, with WS and WP achieving grafting degrees of 58.11% and 64.86%, respectively, alongside elevated browning indices. Secondary structure analysis via circular dichroism revealed substantial protein unfolding, characterized by a reduction in α-helix content (12.85 to 3.25%) and an increase in random coil structures (40.81 to 52.73%). FTIR spectroscopy confirmed covalent bond formation, as evidenced by enhanced O–H and N–H stretching vibrations, contributing to greater conformational stability. Antioxidant activity markedly increased, with WS demonstrating approximately a fourfold enhancement in ABTS radical scavenging capacity (44.11%) compared to native PSP (10.77%), attributed to the formation of Maillard-derived melanoidins. Confocal laser scanning microscopy (CLSM) of emulsions stabilized with WS and WP conjugates revealed smaller and more homogeneous droplet distributions, correlating with higher emulsifying activity indices (WS, 69.70 m<sup>2</sup>/g) and improved emulsion stability (WS, 89.66&#xa0;min), mediated by steric and electrostatic stabilization mechanisms. Thiobarbituric acid reactive substances (TBARS) analysis indicated reduced lipid oxidation in WS-stabilized emulsions after 14&#xa0;days of storage (0.632 vs. 0.883 TBA value/g for PSP). Rheological characterization demonstrated viscoelastic dominance (<i>G</i>′ &gt; <i>G</i>″) and shear-thinning behavior in WS and WP emulsions, indicative of strong network formation. These findings provide critical mechanistic insights into the design of plant-based Maillard conjugates as novel food-grade stabilizers for clean-label emulsion systems.</p>

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Maillard-Type Conjugates of Pumpkin Seed Protein with Different Polysaccharides as Novel Emulsion Stabilizers: Structure–Function Relationships and Emulsifying Performance

  • St. Nur Hikmah,
  • Nurul Saadah Said,
  • Won Young Lee

摘要

This study investigates how Maillard-induced structural reorganization of pumpkin seed protein isolate (PSP) conjugated with different types of polysaccharides, pectin (WP), gum arabic (WG), and sodium alginate (WS) governs emulsion functionality and oxidative stability. Conjugates synthesized via wet heating exhibited advanced glycation, with WS and WP achieving grafting degrees of 58.11% and 64.86%, respectively, alongside elevated browning indices. Secondary structure analysis via circular dichroism revealed substantial protein unfolding, characterized by a reduction in α-helix content (12.85 to 3.25%) and an increase in random coil structures (40.81 to 52.73%). FTIR spectroscopy confirmed covalent bond formation, as evidenced by enhanced O–H and N–H stretching vibrations, contributing to greater conformational stability. Antioxidant activity markedly increased, with WS demonstrating approximately a fourfold enhancement in ABTS radical scavenging capacity (44.11%) compared to native PSP (10.77%), attributed to the formation of Maillard-derived melanoidins. Confocal laser scanning microscopy (CLSM) of emulsions stabilized with WS and WP conjugates revealed smaller and more homogeneous droplet distributions, correlating with higher emulsifying activity indices (WS, 69.70 m2/g) and improved emulsion stability (WS, 89.66 min), mediated by steric and electrostatic stabilization mechanisms. Thiobarbituric acid reactive substances (TBARS) analysis indicated reduced lipid oxidation in WS-stabilized emulsions after 14 days of storage (0.632 vs. 0.883 TBA value/g for PSP). Rheological characterization demonstrated viscoelastic dominance (G′ > G″) and shear-thinning behavior in WS and WP emulsions, indicative of strong network formation. These findings provide critical mechanistic insights into the design of plant-based Maillard conjugates as novel food-grade stabilizers for clean-label emulsion systems.