ArticleAdvanced biomedical research2014
Cloning, expression, purification and characterisation of Erwinia carotovora L-asparaginase in Escherichia coli.
Article in Advanced biomedical research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 43 citations in OpenAlex.
- Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent.Microbial cell factories · 2025Article
- Toward Safer Biotherapeutics: Expression and Characterization of a Humanized Chimeric L-Asparaginase inInternational journal of molecular sciences · 2025Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- Improvement of recombinant L-Asparaginase production in3 Biotech · 2023Article
- L-Asparaginase fromPharmaceuticals (Basel, Switzerland) · 2022Article
- Overview of the structure, side effects, and activity assays of l-asparaginase as a therapy drug of acute lymphoblastic leukemia.RSC medicinal chemistry · 2022Review
- Highly Active Thermophilic L-Asparaginase fromInternational journal of molecular sciences · 2021Article
- A Novel L-Asparaginase from Hyperthermophilic ArchaeonInternational journal of molecular sciences · 2021Article
- Development of Processes for Recombinant L-Asparaginase II Production byPharmaceutics · 2020Article
- Functional and structural evaluation of the antileukaemic enzyme L-asparaginase II expressed at low temperature by different Escherichia coli strains.Biotechnology letters · 2020Article
- L-Asparaginase from Erwinia carotovora: insights about its stability and activity.Molecular biology reports · 2019Article
- Expression and Functional Characterization of Pseudomonas aeruginosa Recombinant L.Asparaginase.The protein journal · 2018Article
- Simultaneous cell disruption and semi-quantitative activity assays for high-throughput screening of thermostable L-asparaginases.Scientific reports · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundFor the past 30 years, bacterial L-asparaginases have been used as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia. It is found in a variety of organisms such as microbes, plants and mammals. Their intrinsic low-rate glutaminase activity, however, causes serious side-effects, including neurotoxicity, hepatitis, coagulopathy and other dysfunctions. Erwinia carotovora asparaginase shows decreased glutaminase activity, so it is believed to have fewer side-effects in leukemia therapy. Our aim was to clone, express, purify and characterize E. carotovora asparaginase. MATERIALS AND
methodsL-asparaginase from E. carotovora NCYC 1526 (ErA) was cloned and expressed in Escherichia coli strain BL21 (DE3). The enzyme was purified to homogeneity by affinity chromatography. Various conditions were tested to maximize the production of recombinant asparaginase in E. coli.
resultsA new L. asparaginase from E. carotovora NCYC 1526 (ErA) was successfully cloned, expressed and purified in E. coli BL21 (DE3). The specific activity of the enzyme was 430 IU/mg.
conclusionThe results of the present work form the basis for a new engineered form of ErA for future therapeutic use, which could be extended with crystallographic studies.
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