A new genetically derived variant of the glucosyltransferase from Streptococcus oralis has been characterized physicochemically and kinetically. Compared with the industrially used glucosyltransferase from Leuconostoc mesenteroides, the enzyme variant GTF-R S628D possesses 25 times higher affinity for the specific glucosylation of glucose. For a concept of integrated reaction and product isolation, a fluidized bed reactor with in situ product removal was applied. The technical feasibility and the applicability of the kinetic models for reaction and adsorption could be demonstrated. The immobilized enzyme was stable (20% activity loss after 192 h) and product could be obtained with 90% purity. A bioprocess model was generated which allowed the integral assessment of the enzymatic synthesis and in situ product adsorption.,ne model is a powerful tool which assists with the localization of optimal process parameters. It was applied for the process evaluation of other glucosyltransferases and demonstrated key characteristics of each enzymatic system.