Effect of tyrosinase‐catalyzed crosslinking on the structure and allergenicity of turbot parvalbumin mediated by caffeic acid
Shenglan Tian, Jiaju Ma, Ishfaq Ahmed, Liangtao Lv, Zhenxing Li, Lin Hong, Shenglan Tian, Jiaju Ma, Ishfaq Ahmed, Liangtao Lv, Zhenxing Li, Lin Hong
Journal of the Science of Food and Agriculture
Enzymatic treatment of allergenic protein can alter their functional properties at a mild reaction condition due to specificity of enzymes. Phenolic compounds act as a mediator and enhance the crosslinking reactions. The study aimed to assess the changes in the structure and IgG binding capacity of turbot parvalbumin (PV) upon cross‐linking with tyrosinase (Tyr) in the absence and presence of caffeic acid (CA). SDS‐PAGE analysis revealed the appearance of higher molecular weight bands (24、36 KDa) in the cross‐linked PV. The secondary structure of cross‐linked PV became loosened and disordered. The results of intrinsic fluorescence and ultraviolet (UV) absorption spectral analyses, as well as surface hydrophobicity and free amino group analyses also revealed structural changes. As observed by western blot analysis, the intensity of the PV bands reduced upon Tyr treatment, indicating reduced binding of specific IgG to PV. Moreover, the indirect ELISA analysis confirmed that the IgG binding ability of cross‐linked PV was reduced 34.94 %. Enzymatic treatment mitigated the allergenicity of fish PV, which was closely related to the alterations in the conformational structure. This treatment shown potential for developing hypoallergenic fish products under mild reaction conditions.
Circular dichroism, Secondary structure, Chemical stability, Biochemistry