¹Department of Chemistry, Faculty of Science, University of Sarajevo, Sarajevo, Bosnia and Herzegovina
²Department of Biomedical Sciences, State University of Novi Pazar, Novi Pazar, Srbija
³Department of Biology, Faculty of Science, University of Sarajevo, Sarajevo, Bosnia and Herzegovina
⁴Clinical Center of the University of Sarajevo, Organizational unit clinic for radiology, Sarajevo, Bosnia and Herzegovina Enzymes are catalysts of biological origin, and according to their chemical composition, they are simple or complex proteins. There are several theories about the enzyme's mechanism of action. Today, the Michaelis-Menten theory is generally accepted. According to this theory, during enzymatic reactions, an intermediate compound is created between the enzyme and the substrate. After the formation of this complex, the enzyme catalyzes a chemical reaction that changes the substrate into another molecule, which we call the product. The product is then separated and released from the active site of the enzyme, which is then ready to bind the next substrate molecule. Enzyme activity can be affected by different molecules. The purpose of this study is to use the spectrophotometric approach to determine whether sodium benzoate and ascorbic acid (vitamin C) serve as activators or inhibitors of enzymatic reactions. The obtained results show that both additives bind to the enzyme-substrate complex, causing non-competitive inhibition. Keywords : Enzymes; additives; ascorbic acid; sodium benzoate; inhibition