The glycosylation of α- and δ-tocopherols using Klebsiella pneumoniae and cyclodextrin glucanotransferase (CGTase) was investigated. K. pneumoniae converted α- and δ-tocopherols into the corresponding β-glucosides in 10 and 8% yield, respectively. CGTase glycosylated α-tocopheryl β-glucoside to α-tocopheryl β-maltoside (51%) and α-tocopheryl β-maltotrioside (35%). On the other hand, δ-tocopheryl β-glucoside was converted into the corresponding β-maltoside (45%) and β-maltotrioside (29%) by CGTase. The β-glucoside of α-tocopherol, and β-glucoside and β-maltoside of δ-tocopherol showed inhibitory effects on IgE antibody production and on histamine release from rat peritoneal mast cells.