D-Tagatose 3-epimerase (D-TE) from Pseudomonas sp. ST-24 was immobilized on various types of Chitopearl beads. The highest activity was found in D-TE immobilized on Chitopearl beads of BCW 2503, the yield being about 80% of free enzyme applied. Maximum activity of the immobilized enzyme was obtained at pH 7-9 and around 60 degrees C. The enzyme was stable in a pH range of 7-10, and below 60 degrees C. In a high concentration (30%) of substrate, the reaction progressed without substrate inhibition. Two grams of D-sorbose crystals could be obtained from 3 g D-tagatose. Furthermore, in a batch reaction repeated five times, about 70% of D-tagatose was converted to D-sorbose each time.