Anticancer Activity of L-Asparaginase Produced from Vigna Unguiculata

Moharib, Sorial A.

doi:10.20448/journal.510.2018.51.1.12

Cited by 17 publications

(31 citation statements)

References 45 publications

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“…After 30 min the activity of enzymedepleted. The findings are in close comparison with Moharib (2018) who revealed 30 min optimal reaction time for L-asparaginase extracted from Vigna unguiculata seed.…”

Section: Discussionsupporting

confidence: 82%

“…While the substrate optimal concentration determined from Capascium annum L was 33mM, where catechol was acting as substrate in the mixture (Arnnok et al, 2010). While Moharib (2018) has revealed 200mMoL concentrationof substrate for maximal activity of L asparaginase activity derived from Vigna unguiculata.…”

Section: Discussionmentioning

confidence: 99%

“…Reaction mixture of L-asparaginase obtained from Capsicum annum (fruit) was assayed at different temperatures (15°C, 25°C, 30°C, 35°C, 40°C, 45°C, 50°C and 55°C) and asparagine concentration (10 to 300 mMoL) were studied. The optimization of reaction time required for the maximal quantity of L-asparaginase to stay active for the conversion of L-asparagine to Laspartate was noted from 10 to 90 minutes at optimal temperature and pH (Moharib, 2018).…”

Section: Kinetic Characterization Of Enzymesmentioning

confidence: 99%

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Purification of Robust L-Asparaginase from Capsicum annum and its Therapeutic Efficacy in Leukemia

Ambreen¹

2019

PVJ

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Medicinal plants used for the treatment of chronic diseases, have attracted the interest of scientists. L-Asparaginase is an extracellular enzyme with biomedical significance. The present article discusses the extraction, purification and characterization of L-asparaginase. Enzyme activity was estimated from Chillies (plant of Solanaceae family). Enzyme titer of 112 U/mL was attained from crude extract of Chillies (Capsicum annum) fruit while purified enzyme after gel filtration provided 61.99% yield, activity of 69.43 U/mL and specific activity of 234 U/mg. L-Asparaginase stability was envisaged at optimal pH of 8.6 in the presence of alkaline buffer. Optimal substrate concentration for L-Asparaginase activity was 200 mMoL. The efficacy of purified enzyme was tracked in vivo model. Normal healthy rats were used as control, which were compared with leukemic rats after treatment with enzyme L-Asparaginase. Eventually after treatment with enzyme extract provided best recovery in leukemic model due to high titer of L-Asparaginase, which bears high antineoplastic activity. It may be employed for chemotherapy in tumors such as acute lymphocytic leukemia.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Section: Kinetic Characterization Of Enzymesmentioning

confidence: 99%

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Purification of Robust L-Asparaginase from Capsicum annum and its Therapeutic Efficacy in Leukemia

Ambreen¹

2019

PVJ

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“…6. Effect of some metal ions and EDTA on L-asparaginase activity produced by A. terreus (2018) 48 who reported that cytotoxic activity of L-asparaginase was tested on HELLA, MCF7, HEPG2 and HCT-116 showing that L-aspargenase had higher growth inhibition against Hep-G2 and HCT-116 than Hella and MCF7 carcinoma cell lines. El-Naggar et al (2016) 42 studied the activity of L-asparaginase against CACO 2, HeP 2, HePG 2 cancer cells and reported that IC 50 was 2 -4 U/ml with the highest activity against CACO 2.…”

Section: Cytotoxicity and Anticancer Activities Of The Purified L-aspmentioning

confidence: 99%

Purification, Characterization and Anticancer Activity of L-asparaginase Produced by Marine Aspergillus terreus

Hassan¹,

Farag²,

Beltagy³

2018

J Pure Appl Microbiol

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L-asparaginase (E.C.3.5.1.1) is an enzyme responsible for hydrolysis of L-asparagine into aspartic acid and ammonia, and has its significant applications in the therapeutics and food technology. It was produced by the marine Aspergillus terreus and precipitated by 65% ammonium sulphate, followed by purification using gel filtration on Sephadex G-100 and DEAE-cellulose ion exchange chromatography, which yielded 11.96 fold purification. The molecular weight of the purified L-asparaginase was approximately 85 kDa, determined by a sodium dodecyl sulphate polyacrylamide gel electrophoresis. L-asparaginase showed high affinity for L-asparagine with a Km of 31.5 mM and Vmax of 500 U/ml. The optimum pH and temperature of the purified enzyme were 5.8 and 40 o C, respectively. The L-asparaginase enzyme was stable from pH 4 to 5.8 and stable up to 70 o C. The effect of activators and inhibitors was studied providing that CdCl 2 , Pb Cl 2 , and Hg Cl 2 strongly inhibited the enzyme activity, while Na Cl highly enhanced activity. Anticancer activity of the purified L-asparaginase was detected against HCT-116, Hep-G2 and MCF-7 cell lines with IC 50 ranged from 3.79-12.6 µg/ml.

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“…L-ASP induces cytotoxicity by breaking asparagine into L-aspartate and ammonia. According to Moharib, the cytotoxic activity of L-ASP is closely related to asparagine, and the asparagine level differed among various cell lines [30]. erefore, L-ASP induced cancer cell death to varying degrees.…”

Section: Cytotoxicity Activitiesmentioning

confidence: 99%

Nanoliposomal L-Asparaginase and Its Antitumor Activities in Lewis Lung Carcinoma Tumor-Induced BALB/c Mice

Thao

Nguyen

et al. 2019

Advances in Materials Science and Engineering

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Although L-Asparaginase (L-ASP) is an effective chemotherapeutic agent, it has side effects such as fever, skin rashes, chills, anaphylaxis, and severe allergic reactions. Moreover, the short half-life of L-ASP reduces its antitumor activity. To reduce its side effects and broaden its pharmaceutical applications, L-ASP obtained from Pectobacterium carotovorum was subjected to liposomal conjugation. The enzyme was then loaded into liposomes using the hydrated thin-film method. The in vitro cytotoxic activity of liposomal L-ASP was evaluated with the MTT assay using cancerous cell lines, and its antitumor effects were examined in Lewis lung carcinoma (LLC) tumorized mice. The average size of the liposomes containing purified L-asparagine was 93.03 ± 0.49 nm. They had a zeta potential of –15.45 ± 6.72 mV, polydispersity index of 0.22 ± 0.02, and encapsulation efficiency of 53.99 ± 5.44%. The in vitro cytotoxic activity of liposomal L-ASP was less effective against LLC, MCF-7 (human breast carcinoma), HepG2 (human hepatocellular carcinoma), SK-LU-1 (human lung carcinoma), and NTERA-2 (pluripotent human embryonic carcinoma) cells than that of free L-ASP. However, the antitumor activity of liposomal L-ASP was significantly greater than that of untrapped L-ASP at the same doses (6 UI/mouse) in terms of tumor size (6309.11 ± 414.06 mm3) and life span (35.00 ± 1.12 days). This is the first time the antitumor activities of PEGylated nanoliposomal L-ASP have been assessed in LLC carcinoma tumor-induced BALB/c mice and showed significantly improved pharmacological properties compared to those of free L-ASP (P<0.05). Thus, nanoliposomal L-ASP should be considered for its widening applications against carcinoma tumors.

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Anticancer Activity of L-Asparaginase Produced from Vigna Unguiculata

Cited by 17 publications

References 45 publications

Purification of Robust L-Asparaginase from Capsicum annum and its Therapeutic Efficacy in Leukemia

Purification of Robust L-Asparaginase from Capsicum annum and its Therapeutic Efficacy in Leukemia

Purification, Characterization and Anticancer Activity of L-asparaginase Produced by Marine Aspergillus terreus

Nanoliposomal L-Asparaginase and Its Antitumor Activities in Lewis Lung Carcinoma Tumor-Induced BALB/c Mice

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