Abstract: Taking parvalbumin (PV) from silver carp as the research object, four different reducing sugars-glucose, ribose, maltose and maltotriose, were selected to noncovalently with PV. High performance liquid chromatography combined with size exclusion chromatography, ultraviolet absorption, fluorescence spectroscopy, enzyme-linked immunosorbent assay and molecular docking were used to characterize the molecular weight, structure and allergenicity of PV to explore the effect of different reducing sugars based on noncovalent interaction on the structure and allergenicity of PV. The results indicated that glucose, ribose, maltose and maltotriose could be noncovalently bound to the hydrophobic cavity of PV, mainly through hydrogen bonds and hydrophobic interactions, with the lowest binding energies of −4.03, −4.01, −3.73 and −2.33 kcal/mol, respectively. This noncovalent binding could change the structure of PV, manifested as a decrease in ultraviolet absorption intensity, synchronous and intrinsic fluorescence intensity, and a reduction in the binding ability of silver carp PV to IgE. Therefore, different reducing sugars could mask the allergenic epitopes of silver carp PV through noncovalent interaction, reducing its allergenicity. The results of this study aim to provide a theoretical basis for reducing the sensitization of PV and expanding the application range of fish products.