The effect of glycation of potato proteins on their immunoreactivity was studied by using a pool of human sera with specific IgE to potato proteins. Patatin conjugates were more immunoreactive than protease inhibitors ones. To better understand this behavior, the changes in patatin structure upon glycation and heat treatment were investigated. Patatin demonstrated an increase in total immunoreactivity when glycated with galactose and galactooligosaccharides. However, galactan conjugation to patatin resulted in a decrease in immunoreactivity by restricting IgE's access to the epitopes. Although the heat treatment resulted in a decrease in patatin's immunoreactivity through aggregation, it was less effective when patatin conjugates were used due to the decrease in aggregation and the secondary structural changes. Upon digestion, native patatin exhibited the largest decrease in immunoreactivity resulting from the disruption of both conformational and sequential epitopes. Patatin conjugates were less digested and had higher IgE-immunoreactivity as compared to the digested patatin.