Purification and characterization of lysozyme in Persian sturgeon, Acipenser persicus (Borodin, 1897) from the Southwest Caspian Sea
نویسندگان
1 Department of Biology, Faculty of Science, University of Guilan, Rasht, Iran
2 Genetic and Biotechnology Department, International Sturgeon Research Institute, Rasht, Iran
3 Department of Biology, Faculty of Science, University of Guilan, Rasht, Iran
4 Department of Biology, Faculty of Science, University of Guilan, Rasht, Iran
5 Department of Chemistry, Faculty of Science, Islamic Azad University of Guilan, Rasht, Iran
doi
10.22124/cjes.2018.3204چکیده
Lysozyme (N-acetylmuramide glyconohydrolase, (EC 3.2.1.17)) is a unique enzyme which cleaves the β-1,4 linkages of N-acetylmuramic and N-acetylglucosamine of the peptidoglycan, which leads to the lysis of the bacterial cell wall. Lysozyme, as a self-defense enzyme, is produced in many organs of vertebrates. The present study describes purification and characterization of lysozyme from Acipenser persicus (Borodin, 1897). After the extraction process, ion exchange chromatography was utilized to purify the enzyme. The SDS-PAGE analysis confirmed that the molecular weight was about 14 kDa. Moreover, some of the biochemical properties such as optimum temperature, pH and the effect of metal ions on the activity of purified enzyme were investigated. Based on the results the optimum activity and pH were obtained at 50 °C and 6.5 respectively. The purified lysozyme was active in the presence of different salts including NaCl (0–0.125 M), KCl (0.075–0.125 M), MgCl2, and CaCl2 (0.005 M). Kinetic parameters were also calculated.
