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Electron beam-induced structural modification enhances pea protein emulsion gels formed by transglutaminase‑calcium
Yan Yin1, Siqi Wang1, Jiangtao Yu2
1College of Food Science and Engineering, Northwest A&F University, Yangling 712100, Shaanxi, China.
Abstract:
Pea protein isolate (PPI) has limited use in the food industry due to its poor solubility and gelation. This study used electron beam irradiation (EBI, 5-30 kGy) to treat PPI, followed by dual crosslinking with transglutaminase (TG) and/or CaCl2 to prepare oil-in-water emulsion gels, aiming to optimize processing conditions for improved gelation properties. Moderate EBI (10-15 kGy, with 15 kGy showing the greatest overall improvement) promoted protein unfolding and increased surface hydrophobicity, water solubility (10.6% → 11.2%), and emulsifying activity index (15.9 → 25.6 m2/g). Dual crosslinking (TG + 25 mM Ca2+) generated stronger, more elastic networks than single crosslinking, with higher water-holding capacity (80.7%), superior freeze-thaw stability, and higher viscoelasticity. EBI-treated PPI produced softer yet more hydrated gels. Excessive Ca2+ (≥50 mM) or irradiation (20-30 kGy) increased protein aggregation and weakened gel strength. This combined physical-enzymatic crosslinking strategy allows tailoring of plant-based emulsion gels for specific food applications.
