ArticlePloS one2014
Purification and characterization of a novel and robust L-asparaginase having low-glutaminase activity from Bacillus licheniformis: in vitro evaluation of anti-cancerous properties.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 170 citations in OpenAlex.
- Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent.Microbial cell factories · 2025Article
- Tapping the untapped: type II L-asparaginase from marine crustacean-derived Chryseomicrobium amylolyticum as a potential bio better for blood cancer therapy.Scientific reports · 2025Article
- Isolation, Identification, and Characterization of L-asparaginase-Producing Human Commensal Bacterial Strains: A Promising Next-Gen Probiotics.Applied biochemistry and biotechnology · 2025Article
- Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- Investigating Functional and Folding Stability of an EngineeredAdvanced pharmaceutical bulletin · 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
- Expression and Biological Evaluation of an Engineered Recombinant L-asparaginase Designed byAdvanced pharmaceutical bulletin · 2023Article
- Characterization of a Type II L-Asparaginase from the HalotolerantLife (Basel, Switzerland) · 2023Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- 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
- Enhancing the Catalytic Activity of Thermo-Asparaginase fromInternational journal of molecular sciences · 2023Article
- Characterizing Non-covalent Protein Complexes Using Asymmetrical Flow Field-Flow Fractionation On-Line Coupled to Native Mass Spectrometry.Analytical chemistry · 2023Article
- Thermo-L-Asparaginases: From the Role in the Viability of Thermophiles and Hyperthermophiles at High Temperatures to a Molecular Understanding of Their Thermoactivity and Thermostability.International journal of molecular sciences · 2023Review
- Aliivibrio fischeri L-Asparaginase production by engineered Bacillus subtilis: a potential new biopharmaceutical.Bioprocess and biosystems engineering · 2022Article
- Recombinant production and characterization of L-glutaminase (glsA) as a promiscuity therapeutic enzyme.Applied microbiology and biotechnology · 2022Article
- Microbial L-asparaginase as a promising enzyme for treatment of various cancers.Applied microbiology and biotechnology · 2022Review
- Molecular cloning, characterization, and in-silico analysis of l-asparaginase from Himalayan3 Biotech · 2022Article
- Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions.Pharmaceutics · 2022Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L-asparaginase having low glutaminase has been a key therapeutic agent in the treatment of acute lymphpoblastic leukemia (A.L.L). In the present study, an extracellular L-asparaginase with low glutaminase activity, produced by Bacillus licheniformis was purified to homogeneity. Protein was found to be a homotetramer of 134.8 KDa with monomeric size of 33.7 KDa and very specific for its natural substrate i.e. L-asparagine. The activity of purified L-asparaginase enhanced in presence of cations including Na+ and K+, whereas it was moderately inhibited in the presence of divalent cations and thiol group blocking reagents. The purified enzyme was maximally active over the range of pH 6.0 to 10.0 and temperature of 40°C and enzyme was stable maximum at pH 9.0 and -20°C. CD spectra of L-asparaginase predicted the enzyme to consist of 63.05% α-helix and 3.29% β-sheets in its native form with T222 of 58°C. Fluorescent spectroscopy showed the protein to be stable even in the presence of more than 3 M GdHCl. Kinetic parameters Km, Vmax and kcat of purified enzyme were found as 1.4×10(-5) M, 4.03 IU and 2.68×10(3) s(-1), respectively. The purified L-asparaginase had cytotoxic activity against various cancerous cell lines viz. Jurkat clone E6-1, MCF-7 and K-562 with IC50 of 0.22 IU, 0.78 IU and 0.153 IU respectively. However the enzyme had no toxic effect on human erythrocytes and CHO cell lines hence should be considered potential candidate for further pharmaceutical use as an anticancer drug.
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