Purification, Kinetic Properties and Antitumor Activity of L-Glutaminase from Penicillium brevicompactum NRC 829
Ali Mohamed Elshafei, Mohamed Mohamed Hassan1, Nadia Hussein Ali, Mohamed Abd-Elmontasr Abouzeid, Dalia Ali Mahmoud, Dina Helmy Elghonemy
Microbiology Research Journal International · pp. 97–115 · Published 16 Oct 2013
10.9734/BMRJ/2014/5098Abstract
Aim: The aims of the present study were to purify and characterize L-glutaminase from Penicillium brevicompactum NRC 829; and to evaluate the antitumor activity of the purified enzyme against different tumor human cell lines. Study Design: Testing of antitumor activity of L-glutaminase, purified from a filamentous fungal strain, against four different tumor human cell lines. Place and Duration of Study: Department of Microbial Chemistry, Genetic Engineering and Biotechnology Division, National Research Centre (NRC), Cairo, Egypt, between January 2011 and February 2012. Methodology: P. brevicompactum NRC 829 was grown and maintained on modified Czapek Dox agar (MCD) medium. Cell-free extract was directly used as the source of crude enzyme. L-glutaminase was purified by heat treatment for 20 min at 50ºC, followed by gel filtration on Sephadex G-100 and G-200 columns. Results: An intracellular L-glutaminase from Penicillium brevicompactum NRC 829 was purified to homogeneity (162.75 fold) with an apparent molecular mass (Mr) of 71 kDa. The purified enzyme showed its maximal activity against L-glutamine when incubated at pH 8.5 at 50ºC for 30 min. The purified enzyme retained about 92 % of its initial activity after incubation at 70ºC for 30 min indicating the thermo-stability nature of this enzyme. The highest activity was reported towards its natural substrate, L-glutamine, with an apparent Km value of 1.66 mM. The purified enzyme inhibited the growth of human cell line hepatocellular carcinoma (Hep-G2), with IC50 value of 63.3μg/ml. Conclusion: L-glutaminase purified from Penicillium brevicompactum NRC 829 is a potential candidate in food and pharmaceutical industries.
Cited by 50
Atsumi Shimada, Hiroshi Ueno, M. Inagaki · Natural Product Research · 2020
Alyaa M. Abdelhameed, Rana Alqaysi, H. Hilal · Indian Journal of Forensic Medicine & Toxicology · 2020
Hanaa M. Orabi, E. El-Fakharany, Eman S. Abdelkhalek · Preparative Biochemistry & Biotechnology · 2019
T. M. Maharem, M. Emam, Youssef A. Said · International Journal of Biological Macromolecules · 2019
Hanaa M. Orabi, E. El-Fakharany, Eman S. Abdelkhalek · Journal of Microbiology, Biotechnology and Food Sciences · 2019
Olatunji Olarewaju Musa, Chukwuemeka Nzelibe Humphrey · African Journal of Biochemistry Research · 2019
Ayodeji Amobonye, Suren Singh, Santhosh Pillai · Critical Reviews in Biotechnology · 2019
M. Abu-Tahon, G. Isaac · Journal of General and Applied Microbiology · 2019
S. More, R. Swamy, N. Mohan · Proceedings of the National Academy of Sciences, India Section B: Biological Sciences · 2018
T. Sathish, D. Kezia, P. V. Bramhachari · 2018
Related research
- Identification and Characterization of Antibiotic Resistant Bacteria Isolates from In-Patients at the Specialist Hospital, Sokoto, Nigeria — shares topic coverage
- Synthesis, Characterization and Biological Evaluation of Thiazolidinedione Substituted Derivatives — shares topic coverage
- Biochemical Characteristics of Immobilized Chitinase from Alternaria infectoria — shares topic coverage
- Silver Nanoparticles: Biosynthesis, Characterization and Application on Cotton Fabrics — shares topic coverage
- Characterization of Detergent-compatible Alkaline Protease from Bacillus agaradhaerens MTCC 9416 — shares topic coverage
Article metrics
Real usage data collected on this platform.
0
Page views
0
PDF downloads
0
Outbound clicks
50
Citations
Views by country
Approximate, from request IP at view time — not citizenship or institution. Countries with fewer than 5 views are grouped as "Other".
No views recorded yet.
Traffic sources
Referring site, by host.
No traffic recorded yet.
Views and downloads exclude known bots/crawlers. Citations combines this platform's own DOI-resolved index with each external source's own reported total — see Cited by above for individually listed citing works. Last refreshed 0 seconds ago.