Biocatalysis represents the application of enzymes to accelerate a chemical reaction from which the enzymes themselves exit unchanged. Enzymes are extremely important biological molecules in the pharmaceutical industry, because they possess significant regio-, chemo- and stereoselectivity and allow obtaining pure active pharmaceutical components. Halohydrin-dehalogenase (HHDH) is one of the more interesting enzymes in the field of obtaining these components. These enzymes, which belong to the group of lyases, are extremely important industrial enzymes that can be used in the synthesis of optically active epoxides, β-substituted alcohols, as well as chiral tertiary alcohols, and nowadays are mostly obtained by overexpression in recombinant Escherichia coli cells. In order to improve properties of the enzymes, enzymes are subjected to the process of immobilization on a carrier or without a carrier by cross-linking. Immobilized enzymes have proven to be extremely effective for commercial use due to lower costs of the process, greater stability and the possibility of recycling the enzyme. One of the available immobilization methods is the immobilization of enzymes or whole cells in a polymer matrix of calcium alginate, which has various advantages such as mild polymerization conditions, non-toxicity, biocompatibility, economical advantages and resistance to contamination by various microorganisms. Organic fluorinated compounds are extremely important building molecules in the pharmaceutical, agronomic and functional materials industry. They show different unique physical, chemical and biological properties compared to non-fluorinated compounds, however their availability results almost entirely from artificial synthesis. Due to this, as well as due to the need for development of green industry, enzymes are included in their production, the use of which leads to energy savings, contributes to environmental protection, safety, high process selectivity, etc. In this work, the process of immobilization of recombinant Escherichia coli cells containing the HheC-ISM4 enzyme on alginate beads was successfully carried out, with which the synthesis reaction of (S)-2-(4-fluorophenyl)-3-hydroxypropanonitrile was successfully carried out in a rotating bed reactor. High product yield was obtained, 98.87%, as well as high conversion of the substrate, 75.61%, and high optical purity expressed through the enantiomeric residue of the substrate, 87.61%.