During the heating process, the amino acid asparagine, which is naturally present in starchy foods, undergoes a chemical process called the Maillard reaction. This reaction is the main cause of browning and crisping of baked or fried foods. Unfortunately, carcinogens such as acrylamide and some heterocyclic amines are also formed during the Maillard reaction. Apart from its numerous applications, acrylamide is a known toxin that causes a range of toxicities. These adverse effects include its damaging effects on the nervous system, fertility, and the possibility of mutagenic and carcinogenic effects through the production of epoxides (glycidamides). Asparaginase is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid (Figure 1). The presence of asparaginase has been reported in various organisms, including animals, plants, and microorganisms (bacteria, fungi, algae, yeasts, and actinomycetes) other than humans. In the food industry, the use of asparaginase reduces acrylamide production. The aim of this study is to investigate the kinetic properties of the asparaginase enzyme and inhibit acrylamide production in the Maillard reaction. In this study, the asparaginase enzyme was partially isolated from the liver using homogenization, centrifugation, precipitation with ammonium sulfate, and dialysis at 4°C. After extraction, the enzyme activity was estimated by the Nessler reagent (2). In this study, the specific activity of the asparaginase enzyme isolated from the liver was determined to be 2.77 U/mg. The optimum pH of the enzyme was 6.5 and the optimum temperature was 35°C. The kinetic parameters Km and Vmax of the enzyme were 127.295 mM and 3.639 mM/min, respectively. Since the asparaginase enzyme can reduce acrylamide in the food industry, the study of the kinetics of this enzyme under different conditions such as ions, natural compounds, etc. should be of interest to researchers for more extensive studies.
