L-asparaginase, acrylamide quenching enzyme production from leaves of Tamarindus indica and seeds of Vigna radiata–Fabaceae

Ambreen, Aisha; Zia, Muhammad Anjum; Asger, Muhammad; Muhammad, Faqir

doi:10.30848/pjb2020-1(42)

Cited by 5 publications

(7 citation statements)

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“…The fractions collected were also analyzed spectrophotometrically at 540 nm. 8 Assay for L-asparaginase by Nesslerization. The enzymatic assay was performed using L-asparagine as substrate, and hydrolysis was undertaken by the Nessler method using phosphate buffer.…”

Section: Purification Of L-asparaginasementioning

confidence: 99%

“…Healthy cells escape this shortage of asparagine as they recover by supplying Asn’ from L-Asparaginase synthetase. 8 Commercially, the anticancer enzyme for clinical application is obtained from Escherichia coli and Erwinia caroto v ora, commonly marketed as Elspar, Oncaspar, Erwinase, and Kidrolase, which induce therapeutic reactions and side effects. 9 - 11 To avoid adverse anaphylaxis and therapeutic reactions, the anticancer enzyme L-asparaginase was elucidated from a phytomedicinal source.…”

Section: Introductionmentioning

confidence: 99%

“… 12 As far as enzyme concentration is concerned, a markedly high concentration of L-asparaginase from Vigna radiata and Tamarindus indica ( Fabaceae ) is also reported. 8 Solanum nigrum , 13 a phytomedicinal source well known as “Black Nightshade” and “Makoh,” 14 belongs to the genus Solanum, family Solanaceae 15 SN world widely employed for disparate ailments, including seizure and epilepsy, pain, ulcer, inflammation, diarrhea, some eye infections, and jaundice. 14 SN (fruit and leaf parts) contains flavonoids, phenolic compounds, tocopherols, polysaccharides, glycoalkaloids, and glycoproteins well-known to produce antiproliferative effects due to their immunomodulatory properties.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Anticancer L-Asparaginase and Phytoactive Compounds From Plant Solanum nigrum Against MDR (Methicillindrug resistant) Staphylococcus aureus and Fungal Isolates

et al. 2022

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L-asparaginase is used in chemotherapy for acute lymphoblastic leukemia and other cancers. L-asparaginase derived from bacterial source triggers immune responses. The current study investigates Solanum nigrum as a novel and latent source of L-asparaginase to minimize immunological reactions. The antitumor activity of SN methanol extract was determined using the potato disc assay. InterPro Chimera and InterPro were used to predict the amino acid sequence of L-asparaginase and its anticancer activity. Purification of the enzyme was carried out to homogeneity of 1.51-fold with a recovery of 61.99%. At optimal conditions of 36.5°C, pH 8.6, and 8.5 g/mL substrate, fruit (crude extract) revealed an L-asparaginase titer of 48.23 U/mL. The molecular weight of the enzyme was calculated to be 32 ± 5 kDa using SDS PAGE. The fruit’s total flavonoids and phenolic contents are 0.42 ± .030 g/mL and 94 ± 1.9 mg CAE, respectively. Anti-tumorigenic efficacy was determined to be 66% against Agrobacterium tumefaciens. Additionally, the extract possesses potent antifungal and antibacterial properties. Molecular docking provided the structural motifs and underlying interactions between L-asparaginase, N-acetylglucosamine, murine, and chitin. SN contains high levels of the enzyme L-asparaginase and phytochemicals, making it a potential source of anticancer drugs.

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Section: Purification Of L-asparaginasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Anticancer L-Asparaginase and Phytoactive Compounds From Plant Solanum nigrum Against MDR (Methicillindrug resistant) Staphylococcus aureus and Fungal Isolates

et al. 2022

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“…L-asparaginases are classified into I and II subtypes based on their structure and intra- and extracellular location [ 2 ]. Both types are widely found in animals, plants, and microorganisms [ 3 , 4 , 5 ]. Among them, type II ASNase has attracted particular attention as an anticancer medication in treating acute lymphoblastic leukemia (ALL) and lymphosarcoma [ 3 ] for its excellent substrate affinity.…”

Section: Introductionmentioning

confidence: 99%

Enhancing the Catalytic Activity of Type II L-Asparaginase from Bacillus licheniformis through Semi-Rational Design

Zhou

Jiao

Shen

et al. 2022

IJMS

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Low catalytic activity is a key factor limiting the widespread application of type II L-asparaginase (ASNase) in the food and pharmaceutical industries. In this study, smart libraries were constructed by semi-rational design to improve the catalytic activity of type II ASNase from Bacillus licheniformis. Mutants with greatly enhanced catalytic efficiency were screened by saturation mutations and combinatorial mutations. A quintuple mutant ILRAC was ultimately obtained with specific activity of 841.62 IU/mg and kcat/Km of 537.15 min−1·mM−1, which were 4.24-fold and 6.32-fold more than those of wild-type ASNase. The highest specific activity and kcat/Km were firstly reported in type II ASNase from Bacillus licheniformis. Additionally, enhanced pH stability and superior thermostability were both achieved in mutant ILRAC. Meanwhile, structural alignment and molecular dynamic simulation demonstrated that high structure stability and strong substrate binding were beneficial for the improved thermal stability and enzymatic activity of mutant ILRAC. This is the first time that enzymatic activity of type II ASNase from Bacillus licheniformis has been enhanced by the semi-rational approach, and results provide new insights into enzymatic modification of L-asparaginase for industrial applications.

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“…L-asparaginase (EC 3.5.1.1) is the enzyme that catalysis the hydrolytic deamination of L-asparagine to produce L-aspartate and ammonia (Pritsa and Kyriakidis, 2001;Borek et al, 2004). The enzyme found in a wide range of prokaryotic and eukaryotic sources (Moharib, 2018;Aisha et al, 2020). Physiologically, L-asparaginase has a vital role in the amino acid catabolism.…”

Section: Introductionmentioning

confidence: 99%

Studies on the recombinant production and anticancer activity of thermostable L- asparaginase I from Pyrococcus abyssi

et al. 2022

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L-Asparaginase catalysing the breakdown of L-Asparagine to L-Aspartate and ammonia is an enzyme of therapeutic importance in the treatment of cancer, especially the lymphomas and leukaemia. The present study describes the recombinant production, properties and anticancer potential of enzyme from a hyperthermophilic archaeon Pyrococcus abyssi. There are two genes coding for asparaginase in the genome of this organism. A 918 bp gene encoding 305 amino acids was PCR amplified and cloned in BL21 (DE3) strain of E. coli using pET28a (+) plasmid. The production of recombinant enzyme was induced under 0.5mM IPTG, purified by selective heat denaturation and ion exchange chromatography. Purified enzyme was analyzed for kinetics, in silico structure and anticancer properties. The recombinant enzyme has shown a molecular weight of 33 kDa, specific activity of 1175 U/mg, KM value 2.05mM, optimum temperature and pH 80°C and 8 respectively. No detectable enzyme activity found when L-Glutamine was used as the substrate. In silico studies have shown that the enzyme exists as a homodimer having Arg11, Ala87, Thr110, His112, Gln142, Leu172, and Lys232 being the putative active site residues. The free energy change calculated by molecular docking studies of enzyme and substrate was found as ∆G – 4.5 kJ/mole indicating the affinity of enzyme with the substrate. IC50 values of 5U/mL to 7.5U/mL were determined for FB, caco2 cells and HepG2 cells. A calculated amount of enzyme (5U/mL) exhibited 78% to 55% growth inhibition of caco2 and HepG2 cells. In conclusion, the recombinant enzyme produced and characterized in the present study offers a good candidate for the treatment of cancer. The procedures adopted in the present study can be prolonged for in vivo studies.

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L-asparaginase, acrylamide quenching enzyme production from leaves of Tamarindus indica and seeds of Vigna radiata–Fabaceae

Cited by 5 publications

References 0 publications

Anticancer L-Asparaginase and Phytoactive Compounds From Plant Solanum nigrum Against MDR (Methicillindrug resistant) Staphylococcus aureus and Fungal Isolates

Anticancer L-Asparaginase and Phytoactive Compounds From Plant Solanum nigrum Against MDR (Methicillindrug resistant) Staphylococcus aureus and Fungal Isolates

Enhancing the Catalytic Activity of Type II L-Asparaginase from Bacillus licheniformis through Semi-Rational Design

Studies on the recombinant production and anticancer activity of thermostable L- asparaginase I from Pyrococcus abyssi

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