Abstract: In this paper,the glycosylation of ginkgo seed protein (GSP) and glucose was carried out by moist heat,in order to reduce the immunogenicity of ginkgo protein. The process of glycosylation was optimized by enzyme-linked immunosorbent assay for detection of immunogenicity. The UV absorption,endogenous fluorescence emission and secondary structure changes of GSP were analyzed to study the effect of glycosylation reaction on its structure. The results showed that the ratio of protein to sugar,glycosylation temperature and time were 1:3,90℃ and 60 min,respectively. Under this condition,the immunogenicity of GSP was effectively reduced by 54%. At the same time,glycosylation could increase the exposure of UV-absorption amino acid residues and reduce the number of surface fluorescent emission groups. Meanwhile,glycosylation increased the content of α-helix and random curl in GSP,and reduced the content of β-fold and corner.