ArticlePoultry science2025
Structural and techno-functional properties of pH-shifted protein isolates from unhatched hen eggs.
Article in Poultry science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Genotype-Dependent Variations in Egg Quality and Nutritional Composition of Thermotolerant Chickens Under Hot-Climate Conditions.Food science & nutrition · 2026Article
- Physicochemical and Structural Characterization of Composite Gels of Commercial Hemp Seed Protein Concentrate and Hemp Seed Protein Hydrolysate.Gels (Basel, Switzerland) · 2026Article
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Authors and funding
7 authors.
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Abstract
This study explores the effects of pH-shift processing (acid and alkaline) on the physicochemical and techno-functional properties of protein isolates (PPI) from unhatched hen eggs-infertile (INF) and dead-in-shell (DIS)-compared to commercial whole hen egg powder (CEP). Structural changes were evident in PPI, with reduced reactive SH content and surface hydrophobicity relative to CEP (p < 0.05). Thermal denaturation temperature (Td) varied by egg type and pH treatment, with DIS alkaline-PPI exhibiting the highest Td (p < 0.05). While CEP demonstrated superior solubility, DIS alkaline-PPI exhibited higher viscosity (p < 0.05). Foamability was highest in CEP (p < 0.05), yet PPI, particularly acid-INF-PPI, showed enhanced foam stability. CEP had the highest emulsifying activity index (EAI), whereas DIS alkaline-PPI displayed superior emulsion stability index (ESI) (p < 0.05). Gel formation was concentration-dependent; CEP formed a soft gel at 20% protein, whereas all samples gelled at 30%. CEP gels demonstrated significantly greater breaking force, deformation, gel strength, and water-holding capacity (WHC) than PPI gels (p < 0.05), which exhibited a more porous and aggregated microstructure. Rheological analysis revealed that INF alkaline-PPI had the highest storage modulus (G'), indicating strong elasticity; however, CEP exhibited superior mechanical strength, suggesting that a compact protein network enhances resistance to external stress. Acid-extracted PPI displayed lower G', indicating weaker gel formation, while DIS alkaline-PPI showed a delayed gelation process. Loss modulus (G'') and loss tangent (tan δ) further highlighted distinct viscoelastic behaviors across samples. These findings illustrate that the pH-shift process significantly influences the structural and functional properties of unhatched egg PPI, with implications for their application in food formulations.
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