Antibacterial and anticancer activities of (free and immobilized) elastase produced by Klebsiella pneumoniae

Abstract

Elastase is a type of protease that degrades explicitly elastin. The elastase produced by Klebsiella pneumoniae isolates was purified by three steps: ammonium sulfate precipitation, ion-exchange chromatography, and Sephadex G-150 chromatography. The optimal condition for elastase production showed high specific activity with starch (3.8 U/mg protein) and casein as a nitrogen source with a specific activity reaching (3.3 U/mg protein). The maximum elastase production was obtained when the pH value was (7.5) with specific activity (4.4 U/mg protein). Elastase (free and immobilized on TiO2- NPs) was used in application as antibacterial and anticancer, and results showed high antibacterial activity against pathogenic isolates, especially Lactobacillus acidophilus and Pseudomonas aeruginosa were affected by immobilized elastase. Free and immobilized elastase have anticancer activity against lung cancer using the A549 cell line, and immobilized elastase had the potent cytotoxic effect on A549 cells with IC50 142.8 µg/ ml compared with IC50 of normal cell line HdFn on 655.0 µg /ml. Key Words: Klebsiella pneumoniae, Elastase, Immobilization, TiO2-Nps- Antibacterial, Anticancer.