Enzymes are biocatalysts that catalyze reactions in living cells. The possibility of using enzymes outside the cells, in which they are naturally found, has enabled the use of enzymes for industrial purposes. In addition to a number of advantages such as mild reaction conditions and non-toxicity to the environment, the reason for their frequent application is the possibility of producing an optically pure products, which is extremely important in the pharmaceutical industry. Halohydrin-dehalogenase is one of the enzymes that have found application in this field. It can be obtained by overexpression by recombinant DNA technology and shows enantio- and regioselective properties in epoxy ring opening and closing reactions. The aim of this work was to carry out the dehalogenation reaction of 1,3-dichloro-2-propanol catalyzed by the enzyme halohydrin-dehalogenase B type T120A. Prior to the reaction, the enzyme was characterized and its stability in the presence of reaction components was determined. The hydrolysis of the reaction components in the reaction medium and the influence of their concentrations on the kinetics of the enzyme reaction were investigated. From the results, kinetic parameters describing the mathematical model of the enzymatic reaction were obtained. The reaction was performed in a batch reactor. Also, the obtained mathematical model was validated in a batch reactor and as a result the model showed good agreement with the experimental data.