Biochemical characterization of lysozyme from of Rutilus frisii kutum

Lysozyme is a key molecule in innate immune system and plays a vital role in the immune systems of many species against bacterial species with hydrolysis of glycosidic bonds between N-acetylglucosamine and N-acetylmuramicacid of the peptidoglycan layer in the bacterial cell wall and infectional microorganisms. The highest activity of the enzyme in marine species has reported in kidney and spleen. In the present study, lysozyme was extracted from adrenal gland of Caspian Sea Rutilus frisii kutum; then, partially purified by ammonium sulfate and properties such as pH and optimum temperature as well as salt and denaturant concentrations on enzyme activity was evaluated. The enzyme activity was assayed using a suspension of Micrococcus lysodeikticus as substrate. Based on the results, the optimum pH and temperature was found 6 and 45ºC, respectively. Furthermore, lysozyme activity is dependent on salt concentration.