ArticleScientific reports2016
Purification, characterization, cytotoxicity and anticancer activities of L-asparaginase, anti-colon cancer protein, from the newly isolated alkaliphilic Streptomyces fradiae NEAE-82.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- L-asparaginase by filamentous fungi and yeasts from lichens and soils across maritime Antarctic islands.Extremophiles : life under extreme conditions · 2026Article
- Pleurotus ostreatus L-asparaginase's use in food safety and biotechnology: from processing assistance to bioactive agent.Microbial cell factories · 2026Article
- Fungal L-Asparaginase from environmental isolates with antimicrobial and antibiofilm activities.AMB Express · 2026Article
- Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent.Microbial cell factories · 2025Article
- Goan mangrove yeast: a source of therapeutic enzyme L-asparaginase.Folia microbiologica · 2025Article
- Optimizing Gene Sources for L-asparaginase Production: A Comparative Review.Current microbiology · 2025Review
- Cytotoxicity of L-asparaginase from eucaryotic Cladosporium species against breast and colon cancer in vitro.Journal of the Egyptian National Cancer Institute · 2025Article
- The human microbiome: redefining cancer pathogenesis and therapy.Cancer cell international · 2025Review
- Recombinant Esterase (BaCEApplied biochemistry and biotechnology · 2025Article
- Actinomycetes: A Source of Anticancer Metabolites.Current medicinal chemistry · 2025Review
- Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- Aspergillus fumigatus conidial surface-associated proteome reveals factors for fungal evasion and host immunity modulation.Nature microbiology · 2024Article
- The structural insights of L-asparaginase from3 Biotech · 2024Article
- Production of highly cytotoxic and low immunogenic L-asparaginase from Stenotrophomonas maltophilia EMCC2297.AMB Express · 2024Article
- Cloning, expression, and characterization of a novel thermo-acidophilic l-asparaginase of3 Biotech · 2024Article
- l-Asparaginase fromACS omega · 2024Article
- Optimization and characterization of antileukemic L-asparaginase produced by Fusarium solani endophyte.AMB Express · 2023Article
- 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
- Article
- Therapeutic impact of purified Trichoderma viride L-asparaginase in murine model of liver cancer and in vitro Hep-G2 cell line.Journal, genetic engineering & biotechnology · 2023Article
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5 authors.
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Abstract
L-asparaginase is an important enzyme as therapeutic agents used in combination with other drugs in the treatment of acute lymphoblastic leukemia. A newly isolated actinomycetes strain, Streptomyces sp. NEAE-82, was potentially producing extracellular L-asparaginase, it was identified as Streptomyces fradiae NEAE-82, sequencing product was deposited in the GenBank database under accession number KJ467538. L-asparaginase was purified from the crude enzyme using ammonium sulfate precipitation, dialysis and ion exchange chromatography using DEAE Sepharose CL-6B. Further the kinetic studies of purified enzyme were carried out. The optimum pH, temperature and incubation time for maximum L-asparaginase activity were found to be 8.5, 40 °C and 30 min, respectively. The optimum substrate concentration was found to be 0.06 M. The Km and Vmax of the enzyme were 0.01007 M and 95.08 Uml(-1)min(-1), respectively. The half-life time (T1/2) was 184.91 min at 50 °С, while being 179.53 min at 60 °С. The molecular weight of the subunits of L-asparaginase was found to be approximately 53 kDa by SDS-PAGE analysis. The purified L-asparaginase showed a final specific activity of 30.636 U/mg protein and was purified 3.338-fold. The present work for the first time reported more information in the production, purification and characterization of L-asparaginase produced by newly isolated actinomycetes Streptomyces fradiae NEAE-82.
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