ArticleBMC pharmacology & toxicology2018
Purification, characterization and immunogenicity assessment of glutaminase free L-asparaginase from Streptomyces brollosae NEAE-115.
Article in BMC pharmacology & toxicology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 97 citations in OpenAlex.
- Novel glutaminase-free l-asparaginase fromRSC advances · 2026Article
- Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent.Microbial cell factories · 2025Article
- L-asparaginase from the mangrove endophyteToxicology research · 2025Article
- Enhanced production and purification of L-asparaginase from Bacillus paralicheniformis AUMC B-516 with potent cytotoxicity against MCF-7 cell lines.AMB Express · 2025Article
- Cytotoxicity of L-asparaginase from eucaryotic Cladosporium species against breast and colon cancer in vitro.Journal of the Egyptian National Cancer Institute · 2025Article
- L-asparaginase from the novel Fusarium falciforme AUMC 16563: extraction, purification, characterization, and cytotoxic effects on PC-3, HePG-2, HCT-116, and MCF-7 cell lines.BMC microbiology · 2025Article
- Unravelling the outcome of L-glutaminase produced by Streptomyces sp. strain 5 M as an anti-neoplasm activity.Microbial cell factories · 2025Article
- Production of highly cytotoxic and low immunogenic L-asparaginase from Stenotrophomonas maltophilia EMCC2297.AMB Express · 2024Article
- Desirable L-asparaginases for treating cancer and current research trends.Frontiers in microbiology · 2024Review
- Characterization of L-asparaginase from Streptomyces koyangensis SK4 with acrylamide-minimizing potential in potato chips.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Strain improvement, artificial intelligence optimization, and sensitivity analysis of asparaginase-mediated acrylamide reduction in sweet potato chips.Journal of food science and technology · 2023Article
- Production, characterization and techno-economic evaluation of Aspergillus fusant L-asparaginase.AMB Express · 2023Article
- Molecular cloning, characterization, and in-silico analysis of l-asparaginase from Himalayan3 Biotech · 2022Article
- Plant asparaginase versus microbial asparaginase as anticancer agent.Environmental science and pollution research international · 2022Article
- Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions.Pharmaceutics · 2022Review
- Fusarium sp. L-asparaginases: purification, characterization, and potential assessment as an antileukemic chemotherapeutic agent.Environmental science and pollution research international · 2022Article
- Characterization of a Novel L-Asparaginase fromFoods (Basel, Switzerland) · 2021Article
- Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes.Scientific reports · 2021Article
- Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives.Microorganisms · 2021Review
- Molecular Attributes Associated With Refolding of Inclusion Body Proteins Using the Freeze-Thaw Method.Frontiers in microbiology · 2021Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundL-asparaginase is a potential therapeutic enzyme widely used in the chemotherapy protocols of pediatric and adult patients with acute lymphoblastic leukemia. However, its use has been limited by a high rate of hypersensitivity in the long-term used. Hence, there is a continuing need to search for other L-asparaginase sources capable of producing an enzyme with less adverse effects.
methodsProduction of extracellular L-asparaginase by Streptomyces brollosae NEAE-115 was carried out using submerged fermentation. L-asparaginase was purified by ammonium sulphate precipitation and pure enzyme was reached using ion-exchange chromatography, followed by enzyme characterization. Anticancer activity towards Ehrlich Ascites Carcinoma (EAC) cells was investigated in female Swiss albino mice by determination of tumor size and the degree of tumor growth inhibition. The levels of anti-L-asparaginase IgG antibodies in mice sera were measured using ELISA method.
resultsThe purified L-asparaginase showed a total activity of 795.152 with specific activity of 76.671 U/mg protein and 7.835 - purification fold. The enzyme purity was confirmed by using SDS-PAGE separation which revealed only one distinctive band with a molecular weight of 67 KDa. The enzyme showed maximum activity at pH 8.5, optimum temperature of 37 °C, incubation time of 50 min and optimum substrate concentration of 7 mM. A Michaelis-Menten constant analysis showed a K
conclusionsThe study reveals the excellent property of this enzyme which makes it highly valuable for development of chemotherapeutic drug.
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