Purification and characterization of lysozyme in Persian sturgeon, Acipenser persicus (Borodin, 1897) from the Southwest Caspian Sea

Caspian Journal of Environmental Sciences

卷:16

关键词: Catalytic efficiency;    Optimum temperature;    Metal ions;    Ion exchange chromatography;    Acipenser persicus;    Lysozyme;   

DOI  :  

来源: DOAJ

【 摘 要 】

Lysozyme (N-acetylmuramide glyconohydrolase, (EC 3.2.1.17)) is a unique enzyme which cleaves the β-1,4linkages of N-acetylmuramic and N-acetylglucosamine of the peptidoglycan, which leads to the lysis of thebacterial cell wall. Lysozyme, as a self-defense enzyme, is produced in many organs of vertebrates. The presentstudy describes purification and characterization of lysozyme from Acipenser persicus (Borodin, 1897). After theextraction process, ion exchange chromatography was utilized to purify the enzyme. The SDS-PAGE analysisconfirmed that the molecular weight was about 14 kDa. Moreover, some of the biochemical properties such asoptimum temperature, pH and the effect of metal ions on the activity of purified enzyme were investigated. Basedon the results the optimum activity and pH were obtained at 50 °C and 6.5 respectively. The purified lysozyme wasactive in the presence of different salts including NaCl (0–0.125 M), KCl (0.075–0.125 M), MgCl2, and CaCl2 (0.005M). Kinetic parameters were also calculated.

【 授权许可】

Unknown