Malt protein Z (PZ), the main albumin in malt endosperm, exhibits trypsin inhibitory activity and has the ability to bind fat-soluble active molecules. However, its potential utilization as a food ingredient necessitates an evaluation of its allergenicity. Lycopene has many functional activities, such as antioxidant and treatment or alleviation of various diseases, but its tendency to degrade easily hinders its effective utilization. Therefore, this paper investigates the allergenicity of PZ and provides a win-win scenario that PZ interacts with lycopene. PZ interacts with lycopene through non-covalent interactions with a ratio of 4.07 ± 0.20, leading to the formation of homogenous particles with an increased absolute zeta potential, from -7.3 ± 0.2 to -20.0 ± 0.6. Unsurprisingly, the presence of lycopene alleviates the allergenicity of PZ by decreasing the IgE, mMcp-1 and vascular permeability, such as the plasma mMcp-1 decreased from 245.0 ± 5.2 ng/mL for the PZ group to 217.8 ± 4.1 ng/mL for the PZ-LYC group. To uncover the potential mechanism, the linear antigenic epitopes of PZ by ABCpred were predicted, which are almost the potential binding site of lycopene at PZ. On the other hand, PZ improved the storage stability of lycopene. The addition of PZ increased lycopene retention in solution from 14.9 ± 2.7 % to 65.5 ± 2.8 % over 10 days at room temperature with light exposure. These results provide foundations for PZ utilization concerning security, and give ways to protect bioactive molecules.
Keywords: Allergenicity; Interaction; Lycopene; Protein Z; Stability.
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