Abstract: The formation of advanced glycosylation end products (AGEs) in food threatens human health. In this study, we first evaluated the inhibitory effect of spinosin (SP) on the glycosylation of β-lactoglobulin (β-Lg). We explored the inhibitory mechanism by fluorescence spectroscopy, ultraviolet spectroscopy, fourier transform infrared spectroscopy (FTIR), thioflavin-T (Tht) staining, and SDS-PAGE electrophoresis. Fluorescence spectroscopy showed that SP effectively alleviated the formation of AGEs, stabilized the conformational structure of glycosylated β-Lg, and altered the microenvironment near Trp and Tyr residues. UV-visible spectra showed that glycosylation changed the structure of β-Lg，SP can inhibit the production of AGEs by slowing down the process at the end of the Meladic reaction. FTIR spectral analysis showed that hydrogen bonding was involved in the formation of the complexes. The results of Tht showed that SP reduced β-amyloid by attenuating protein misfolding. SDS-PAGE analysis showed that SP-induced cross-linking of glycosylated β-Lg was inhibited. The above results demonstrate that SP is a promising anti-glycosylation agent for use in food systems to reduce the formation of harmful glycosylation products.

Key words: spinosin, anti-glycation, advanced glycosylation end products, β-lactoglobulin, structural changes