A new extracellular glutaminase and urease-free l-asparaginase from Meyerozyma guilliermondii

Ratuchne, Aline; Izidoro, Simone Cristine; Beitel, Susan Michelz; Lacerda, Lorena Tigre; Knob, Adriana

doi:10.1007/s42770-023-00939-x

Cited by 3 publications

(4 citation statements)

References 38 publications

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“…The existence of l -asparaginase was further confirmed by using l -asparaginase-specific antibody, and the enzymatic product from tomato has two subunits with molecular weights of 50 and 30 kDa respectively. The optimum conditions for l -asparaginase activity from tomato are shown to vary with other sources. − …”

Section: Resultsmentioning

confidence: 99%

“…The optimum conditions for l -asparaginase activity from tomato are shown to vary with other sources. 48 − 50 …”

Section: Resultsmentioning

confidence: 99%

“…Positively charged diethylamino ethyl (DEAE)-cellulose resin was used as a matrix because L-Asparaginase is a negatively charged protein. The mobile phase used was the elution buffer consisting of six different concentrations of NaCl solution (25,50,75,100,125, and 150 mM) and 25 mM Tris-HCl. The dialyzed sample was introduced into the column, followed by elution buffer for protein separation.…”

Section: Purification Of L-asparaginasementioning

confidence: 99%

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l-Asparaginase from Solanum lycopersicum as a Nutraceutical for Acute Lymphoblastic Leukemia

Khabade,

Sirigiri,

Ram

2024

ACS Omega

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L-Asparaginase (E.C. 3.5.1.1) is an indispensable analeptic anticancer enzyme used as an amalgam with additional cancer medicines for the cure of acute lymphoblastic leukemia (ALL). The presence of LAparaginase in tomato was confirmed byWestern blotting and DNA sequencing. The L-Asparaginase gene from tomato has been deposited in the NCBI database with accession number: OR736141. Crude enzyme was extracted from the fruit pulp of Solanum lycopersicum, and the activity was determined by the Nesslerization method. Further, the crude extract was subjected to purification, and kinetic parameters were studied. The percentage yield was calculated to be 6.457, and the purification fold was 0.086. The enzyme showed maximum activity at optimum pH 7.0, optimum temperature 37 °C, and incubation time of 05 min. The Michaelis constant "K m " and maximum velocity "V max " values were determined by the Lineweaver−Burk plot, which showed a low K m value of 0.66 and V max of 3.846 IU. Cytotoxic studies were carried out for crude and purified L-asparaginase. Purified L-Asparaginase has exhibited anticancer activity against the ALL model system, K-562 cell line, comparable to that of the anticancer compound vinblastine. Hence, L-Asparaginase from the fruit extract of tomato could be used as a nutraceutical to support cancer treatment in acute lymphoblastic leukemia.

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Section: Resultsmentioning

confidence: 99%

“…The optimum conditions for l -asparaginase activity from tomato are shown to vary with other sources. 48 − 50 …”

Section: Resultsmentioning

confidence: 99%

Section: Purification Of L-asparaginasementioning

confidence: 99%

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l-Asparaginase from Solanum lycopersicum as a Nutraceutical for Acute Lymphoblastic Leukemia

Khabade,

Sirigiri,

Ram

2024

ACS Omega

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“…Many commercial enzymes now use a combination of protein engineering and rational design methods based on computer modeling of proteins, which complements protein engineering and makes it more precise and efficient [16]. L-ASNases for therapeutic use are currently produced exclusively from Escherichia coli and Erwinia chrysanthemi [17], which are FDA-approved drugs [8]. Currently, the World Health Organization (WHO) has included L-ASNase in the list of essential medicines [18].…”

Section: Of 60mentioning

confidence: 99%

Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production

Shishparenok,

Gladilina,

Zhdanov

2023

IJMS

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Genetic engineering for heterologous expression has advanced in recent years. Model systems such as Escherichia coli, Bacillus subtilis and Pichia pastoris are often used as host microorganisms for the enzymatic production of L-asparaginase, an enzyme widely used in the clinic for the treatment of leukemia and in bakeries for the reduction of acrylamide. Newly developed recombinant L-asparaginase (L-ASNase) may have a low affinity for asparagine, reduced catalytic activity, low stability, and increased glutaminase activity or immunogenicity. Some successful commercial preparations of L-ASNase are now available. Therefore, obtaining novel L-ASNases with improved properties suitable for food or clinical applications remains a challenge. The combination of rational design and/or directed evolution and heterologous expression has been used to create enzymes with desired characteristics. Computer design, combined with other methods, could make it possible to generate mutant libraries of novel L-ASNases without costly and time-consuming efforts. In this review, we summarize the strategies and approaches for obtaining and developing L-ASNase with improved properties.

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Antitumor activity of urease-free l-asparaginase with low glutaminase coactivity produced by marine-derived Aspergillus flavus

Nurçe,

Gezgin,

Hameş

2023

Biocatalysis and Agricultural Biotechnology

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A new extracellular glutaminase and urease-free l-asparaginase from Meyerozyma guilliermondii

Cited by 3 publications

References 38 publications

l-Asparaginase from Solanum lycopersicum as a Nutraceutical for Acute Lymphoblastic Leukemia

l-Asparaginase from Solanum lycopersicum as a Nutraceutical for Acute Lymphoblastic Leukemia

Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production

Antitumor activity of urease-free l-asparaginase with low glutaminase coactivity produced by marine-derived Aspergillus flavus

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