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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
