Enantiopure chiral alcohols are used for synthesis of various industrially important chemicals, such as medicines, herbicides, insecticides, etc. One of the most important methods used to produce them is asymmetric reduction of ketones. In this study, (S)-2-hydroxypropiophenone ((S)-2-HPP) was synthesized from benzaldehyde and acetaldehyde. The reaction was catalyzed by the enzyme benzoylformate decarboxylase (BFD) from bacteria Pseudomonas putida. Then, (1S,2S)-1-phenylpropane-1,2-diol ((1S,2S)-1-FPD) was synthesized from (S)-2-HPP. This reaction was catalyzed by the enzyme alcohol dehydrogenase from bacteria Lactobacillus brevis (LbADH). Simultaneously, regeneration of nicotinamide adenine dinucleotide coenzyme (NADH) was carried out by addition of ammonium formate and enzyme formate dehydrogenase from yeast Candida boidinii (CbFDH). The BFD kinetics was described by the double substrate Michaelis – Menten model with a competitive inhibition by the substrate, acetaldehyde. The LbADH kinetics was described by double substrate Michaelis – Menten model with a competitive inhibition by product, NAD+, while the second-order model describes the reverse reaction kinetics. The CbFDH kinetics was described by double substrate Michaelis – Menten model with a competitive inhibition by product, NADH, and substrates from main reactions, (S)-2-HPP and acetaldehyde. The mathematical model was developed and validated in a batch reactor. Two experiments with different initial concentrations of acetaldehyde were carried out. It is concluded that it is better to carry out experiments with higher acetaldehyde concentrations, considering shorter reaction time and the fact that the deactivation of the enzymes is equal in both cases and independent on the acetaldehyde concentration.