ArticleFrontiers in microbiology2014
Refolding and purification of recombinant L-asparaginase from inclusion bodies of E. coli into active tetrameric protein.
Article in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 88 citations in OpenAlex.
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Novel glutaminase-free l-asparaginase fromRSC advances · 2026Article
- Designing strategies for high-level production of peptide-N-glycosidase F (PNGase F) from Flavobacterium meningosepticum using high cell density fed-batch culture of E. coli.Bioprocess and biosystems engineering · 2026Article
- Overcoming challenges in the production of a human-like L-asparaginase: advanced strategies for expression and purification.Biotechnology reports (Amsterdam, Netherlands) · 2026Article
- Expression, Solubilization, and Refolding Recovery of a Novel l‑Asparaginase-Arginase 1 Chimera fromACS omega · 2026Article
- Catalytically active inclusion bodies of cold-adapted lipase: production and its industrial potential.AMB Express · 2025Article
- Expression, Sarkosyl Solubilization, DNase Activity, Purification, and SPR Binding Affinity of Recombinant Diphtheria Toxoid (rCRM197EK) Expressed in Escherichia coli BL21(DE3).Molecular biotechnology · 2025Article
- Optimizing recombinant production of L-asparaginase 1 from Saccharomyces cerevisiae using response surface methodology.Folia microbiologica · 2024Article
- Immunogenic potential and neutralizing ability of a heterologous version of the most abundant three-finger toxin from the coral snakeThe journal of venomous animals and toxins including tropical diseases · 2024Article
- Anti-biofilm potential of human senescence marker protein 30 against Mycobacterium smegmatis.World journal of microbiology & biotechnology · 2023Article
- 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
- Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems.Frontiers in pharmacology · 2023Review
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- African Swine Fever Virus Exhibits Distinct Replication Defects in Different Cell Types.Viruses · 2022Article
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- Quality by Design in Downstream Process Development of RomiplostimIranian biomedical journal · 2022Article
- Human growth hormone inclusion bodies present native-like secondary and tertiary structures which can be preserved by mild solubilization for refolding.Microbial cell factories · 2022Article
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- Solubilization and Refolding of Inclusion Body Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A tetrameric protein of therapeutic importance, Escherichia coli L-asparaginase-II was expressed in Escherichia coli as inclusion bodies (IBs). Asparaginase IBs were solubilized using low concentration of urea and refolded into active tetrameric protein using pulsatile dilution method. Refolded asparaginase was purified in two steps by ion-exchange and gel filtration chromatographic techniques. The recovery of bioactive asparaginase from IBs was around 50%. The melting temperature (Tm) of the purified asparaginase was found to be 64°C. The specific activity of refolded, purified asparaginase was found to be comparable to the commercial asparaginase (190 IU/mg). Enzymatic activity of the refolded asparaginase was high even at four molar urea solutions, where the IB aggregates are completely solubilized. From the comparison of chemical denaturation data and activity at different concentrations of guanidine hydrochloride, it was observed that dissociation of monomeric units precedes the complete loss of helical secondary structures. Protection of the existing native-like protein structure during solubilization of IB aggregates with 4 M urea improved the propensity of monomer units to form oligomeric structure. Our mild solubilization technique retaining native-like structures, improved recovery of asparaginase in bioactive tetrameric form.
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