Interactions between protein Z and lycopene: A win-win scenario for both security and stability

Area of Science:

• Food Science and Technology
• Allergenicity Assessment
• Bioactive Compound Stabilization

Background:

• Malt protein Z (PZ), a major malt albumin, possesses trypsin inhibitory and fat-soluble molecule binding properties.
• PZ's potential as a food ingredient is limited by its allergenicity.
• Lycopene, a beneficial compound, degrades easily, hindering its application.

Purpose of the Study:

• To investigate the allergenicity of malt protein Z (PZ).
• To explore the interaction between PZ and lycopene.
• To assess the impact of this interaction on PZ allergenicity and lycopene stability.

Main Methods:

• Investigated non-covalent interactions between PZ and lycopene.
• Measured changes in particle homogeneity and zeta potential upon complex formation.
• Assessed allergenicity by monitoring IgE, mMcp-1, and vascular permeability.
• Predicted linear antigenic epitopes of PZ using ABCpred.
• Evaluated lycopene retention in solution with and without PZ under ambient conditions.

Main Results:

• PZ and lycopene formed homogenous particles via non-covalent interactions (4.07:1 ratio), increasing absolute zeta potential from -7.3 to -20.0.
• Lycopene significantly alleviated PZ allergenicity, evidenced by decreased IgE, mMcp-1, and vascular permeability.
• PZ addition dramatically improved lycopene storage stability, increasing retention from 14.9% to 65.5% over 10 days.

Conclusions:

• PZ interacts with lycopene, forming stable complexes that reduce PZ's allergenicity.
• The interaction sites for lycopene on PZ correlate with predicted linear antigenic epitopes.
• PZ enhances lycopene's storage stability, offering a strategy for protecting bioactive molecules and validating PZ's safe use in food applications.