ArticleScientific reports2018
Cloning and expression of L-asparaginase from Bacillus tequilensis PV9W and therapeutic efficacy of Solid Lipid Particle formulations against cancer.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent.Microbial cell factories · 2025Article
- Desirable L-asparaginases for treating cancer and current research trends.Frontiers in microbiology · 2024Review
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems.Frontiers in pharmacology · 2023Review
- Immobilization and Characterization of L-Asparaginase over Carbon Xerogels.Biotech (Basel (Switzerland)) · 2022Article
- Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes.Scientific reports · 2021Article
- Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate.RSC advances · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
L-asparaginase, a therapeutic involved in cancer therapy, from Bacillus tequilensis PV9W (ansA gene) was cloned and over expressed in Escherichia coli BL21 (DE3), achieved the aim of maximizing the yield of the recombinant enzyme (6.02 ± 1.77 IU/mL) within 12 h. The native L-asparaginase of B. tequilensis PV9W was encapsulated using solid lipid particles by hot lipid emulsion method, which is reported for first time in this study. Subsequently, the lipid encapsulated L-asparaginase (LPE) was characterized by SEM, UV-Vis spectroscopy, FT-IR, SDS-PAGE and its thermo stability was also analyzed by TGA. Further characterization of LPE revealed that enzyme was highly stable for 25 days when stored at 25 °C, showed high pH (9) tolerance and longer trypsin half-life (120 min). In addition, the cytotoxic ability of LPE on HeLa cells was highly enhanced compared to the native L-asparaginase from Bacillus tequilensis PV9W. Moreover, better kinetic velocity and lower K
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