Biochemical reactions are an integral part of all living organisms and require a higher reaction rate than classical chemical reactions to maintain the normal course of life functions. Enzymes are key elements in the implementation of biocatalysis because they increase the rate of reactions by at least 106 times and greatly facilitate the synthesis and industrial production of substances whose acquisition is significantly more difficult through classical chemical synthesis. They require specific conditions in which they can operate and are present either independently or retained in whole cells and microorganisms. In the organism, they participate in the regulation of homeostasis for the proper functioning of metabolism, energy supply and the formation of proteins, cells and tissue. In this work, the conditions for the enzymatic synthesis of hydroxycinnamic acid amide in an aqueous medium were studied with the aim of determining the optimal conditions for conducting the desired reaction and obtaining the desired product, N-trans-feruloyltyramine. The reaction product belongs to the group of hydroxycinnamic acid amides, which play a role in the proper functioning of plants and have applications in many industries due to their attractive antioxidant, anticancer and anti-inflammatory properties. The enzyme activity was monitored using a spectrophotometer and high-performance liquid chromatography. The influence of pH value, temperature and the addition of ascorbic acid on enzyme activity was determined.