Lactoperoxidase (LPO, E.C.1.11.1.7) is a natural antibacterial agent which is secreted from salivary, mammary, and other mucosal glands. It is one of the crucial enzymes in biological systems, so protection of LPO activity is extremely important for the immune system. Within the scope of this study; in vitro effects of some thiophene-2-sulfonamide derivatives (1a-7a) on bovine milk LPO enzymatic activity were investigated. LPO was purified from the Sepharose-4B-L-tyrosine-5-amino-2-methylbenzenesulfonamide column prepared using affinity chromatography technique with a yield of 169.66 EU/mg specific activity in 452.44 times. As a result, 5-(2-thienylthio) thiophene-2-sulfonamide demonstrated the strongest inhibition impact among these compounds. This molecule has shown a competitive inhibition and it was determined that the IC50 value was 3.4 nM and the Ki value was 2 ± 0.6 nM.
Keywords: Lactoperoxidase; enzyme inhibition; kinetics; purification; thiophene-2-sulfonamide.