Immobilized trypsin covalently attached to cross-linked dextran was prepared. In the presence of high concentrations of primary and secondary alcohols, the transesterification of L-lysine esters catalyzed by the immobilized trypsin was observed to be predominant. In contrast to this, no transesterified product was detected with tertiary butyl alcohol. These reactions were compared with the acid-catalyzed transesterification reactions and the characteristics of the enzymatic reaction are discussed.