Hemocompatible glutaminase free<scp>l</scp>-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression

Shakambari, Ganeshan; Birendranarayan, Anand Kumar; Lincy, Maria Joseph Angelaa; Kumar, Rai Sameer; Ahamed, Quazi Taushif; Ashokkumar, Balasubramaniem; Matheshwaran, Saravanan; Mahesh, Ayyavu; Varalakshmi, Perumal

doi:10.1039/c6ra00727a

Cited by 30 publications

(15 citation statements)

References 29 publications

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“…S5c) as seen by microscopic observation after 12 and 24 h at IC 50 = 0.044 ± 0.006 IU. This value is similar to that of the native L-asparaginase from Bacillus tequilensis PV9W (0.036 ± 0.009 IU) as reported earlier 1 .…”

Section: Resultssupporting

confidence: 90%

“…One such isolate Bacillus tequilensis PV9W is highlighted in the current study. Earlier studies with L-asparaginase from Bacillus tequilensis PV9W showed least K m value when characterized for its substrate L-asparagine and its increased sensitivity to L-asparagine at lower concentration makes it an important enzyme from therapeutic point of view 1 .…”

Section: Introductionmentioning

confidence: 99%

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Cloning and expression of L-asparaginase from Bacillus tequilensis PV9W and therapeutic efficacy of Solid Lipid Particle formulations against cancer

Shakambari

Kumar

Ashokkumar

et al. 2018

Sci Rep

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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 Km values of LPE aided to detect L-asparagine in cell extracts by Differential Pulse Voltammetry (DPV) method. The LPE preparation also showed least immunogenic reaction when tested on normal macrophage cell lines. This LPE preparation might thus pave way for efficient drug delivery and enhancing the stability of L-asparaginase for its therapeutic applications.

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Section: Resultssupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Cloning and expression of L-asparaginase from Bacillus tequilensis PV9W and therapeutic efficacy of Solid Lipid Particle formulations against cancer

Shakambari

Kumar

Ashokkumar

et al. 2018

Sci Rep

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“…Consequently, the depletion of serum Lasparagine by ASNase enzyme leads to tumour cell apoptosis. 2,4 ASNase has another essential use in the food industry, the reduction of acrylamide formation. Acrylamide is a potential human carcinogen, being produced by the reaction of reducing sugars with L-asparagine at high-temperature cooking and in certain starchy foods.…”

Section: Introductionmentioning

confidence: 99%

Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate

et al. 2020

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“…Such a design with three values was formulated for the RSM study of the same isolate. 35 The relationship between the different component factors can be established as a linear or quadratic equation.…”

Section: Methodsmentioning

confidence: 99%

“…The chromatographic purifications were analyzed for the protein at 280 nm (BioPhotometer D30, Eppendorf, Germany). 35 The purified fractions of l -asparaginase were pooled and dialyzed with Tris-HCl (50 mM and pH 8.6) and were stored at −20 °C which were further used to identify the molecular weight of l -asparaginase by SDS-PAGE. 36 The purity of l -asparaginase was determined using the standard molecular weight markers of SDS-PAGE (GeneDireX-BLUltra prestained protein marker).…”

Section: Methodsmentioning

confidence: 99%

Agro Waste Utilization for Cost-Effective Production of l-Asparaginase by Pseudomonas plecoglossicida RS1 with Anticancer and Acrylamide Mitigation Potential

et al. 2017

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Agricultural wastes such as the peels of onion and garlic were used as a supplement along with l-asparagine for the very first time to produce increased yield of l-asparaginase by Pseudomonas plecoglossicida RS1. Statistical optimization strategies such as response surface methodology were used to generate a medium composition containing extracts of 0.9 (v/v) of garlic peel waste and 0.5% (v/v) onion peel waste along with 0.2% (w/w) l-asparagine, which yielded a twofold increase in the enzyme activity compared to the unsupplemented minimal (M-9) medium. The presence of l-asparagine content in the peel extract was confirmed by high-performance liquid chromatography. Further, l-asparaginase was purified to homogeneity, and identity was confirmed by matrix-assisted laser desorption ionization time-of-flight analysis. The application of the purified l-asparaginase as a therapeutic was studied in HeLa cells which showed a p53-mediated G2 cell cycle arrest. Moreover, the purified l-asparaginase showed effective acrylamide mitigation in vitro, at 6 IU, and its effective degradation was also demonstrated by the effect on chemotactic index of Caenorhabditis elegans and the restoration of the cognitive abilities of C. elegans which was coexposed to acrylamide and l-asparaginase compared to that exposed to acrylamide alone. Thus, l-asparaginase, with multipotent applications, was produced by effective waste utilization for economical commercial production.

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Hemocompatible glutaminase freel-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression

Abstract: Glutaminase free l-asparaginase from a marine isolate Bacillus tequilensis PV9W: production, purification, characterization and its biological applications.

Cited by 30 publications

References 29 publications

Cloning and expression of L-asparaginase from Bacillus tequilensis PV9W and therapeutic efficacy of Solid Lipid Particle formulations against cancer

Cloning and expression of L-asparaginase from Bacillus tequilensis PV9W and therapeutic efficacy of Solid Lipid Particle formulations against cancer

Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate

Agro Waste Utilization for Cost-Effective Production of l-Asparaginase by Pseudomonas plecoglossicida RS1 with Anticancer and Acrylamide Mitigation Potential

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