κ-, ι-, and λ-carrageenan Maillard conjugation enhances whey protein isolate stability during ultra-high-temperature treatment.

This study examined Maillard-type conjugation between whey protein isolate (WPI) and three carrageenan (CG) types (κ-, ι-, and λ-CG) to enhance thermal and colloidal stability under ultra-high-temperature (UHT) processing. Conjugates were produced by wet heating (70 °C, 0-12 h) at WPI:CG ratios of 10:1-40:1 and analyzed for structural, compositional (amino acid), and colloidal (ζ-potential, TEM, Turbiscan stability index [TSI]) properties. Maillard conjugation (70°C, 0-12 h) increased denaturation temperature and glycation degree by 5-25%, improving resistance to thermal stress. After UHT treatment, WPI/κ-CG conjugates showed the lowest turbidity and Turbiscan stability index (<2.0) with ζ-potential of -25 to -28 mV. During three weeks of storage, WPI/κ-CG (10:1_6 h) exhibited phase separation, whereas all WPI/λ-CG samples showed protein sedimentation. In contrast, ι-CG conjugates maintain colloidal dispersion with minimal aggregation. These findings demonstrated that κ-CG provided dual-mode stabilization under UHT conditions, while ι-CG ensured superior stability during storage, demonstrating their potential for developing high-protein beverages with tailored viscosity and long-term stability.

• Publication year

  2026

• Venue

  Food Chemistry

• Publication date

  2026-01-01

• Fields of study

  Agricultural and Food Sciences, Medicine, Environmental Science

• Identifiers
  DOI 10.1016/j.foodchem.2026.148246PMID 41633157
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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