Antarctic yeasts as a source of L-asparaginase: Characterization of a glutaminase-activity free L-asparaginase from psychrotolerant yeast Leucosporidium scottii L115

Sánchez‐Moguel, Ignacio; Costa-Silva, Tales A.; Pillaca-Pullo, Omar; Flores-Santos, Juan Carlos; Freire, Rominne Karla Barros; Carretero, Gustavo; Bueno, Júlia da Luz; Camacho-Córdova, D I; Santos, João H. P. M.; Sette, Lara Durães; Pessoa, Adalberto

doi:10.1016/j.procbio.2023.03.003

Process Biochemistry

2023

DOI: 10.1016/j.procbio.2023.03.003

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Antarctic yeasts as a source of L-asparaginase: Characterization of a glutaminase-activity free L-asparaginase from psychrotolerant yeast Leucosporidium scottii L115

Ignacio Sánchez‐Moguel

Tales A. Costa-Silva

Omar Pillaca-Pullo

et al.

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Cited by 4 publications

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L‐Asparaginase from Lachancea Thermotolerans: Effect of Lys99Ala on Enzyme Performance and in vitro Antileukemic Efficacy

Aktar,

Aysan,

Turunen

et al. 2024

Biotechnology Journal

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L‐asparaginases (EC 3.5.1.1) are amidohydrolase enzymes that predominantly catalyze conversion of L‐asparagine to L‐aspartic acid and ammonia. In addition, some exhibit secondary L‐glutaminase activity. Escherichia coli and Erwinia chrysanthemi L‐asparaginases are widely used in the pharmaceutical industry to produce therapeutically important compounds. In the therapeutic use of enzymes, bacterial L‐asparaginases can trigger immune responses, leading to a high rate of adverse effects that diminish the effectiveness of the treatment. This situation has forced scientists to search for promising L‐asparaginases from new sources. Yeast L‐asparaginases could be useful in reducing toxicity and enhancing efficacy but they have been poorly studied to date. Here, we characterized the yeast Lachancea thermotolerans L‐asparaginase (LtASNase) purified by affinity chromatography. It has a specific activity of 313.8 U/mg and a high kcat value (312.4 s). We demonstrated through a semi‐rational design that the mutations of Lys99 show varying effects on catalytic activity, with the Lys99Ala mutant increasing specific activity 3.3‐fold. Furthermore, the in vitro antileukemic activity of the non‐formulated form of Lys99Ala LtASNase was evaluated against SUP‐B15 and REH cell lines. The results demonstrated that LtASNase exhibits significant antileukemic potential, comparable to commercial type II bacterial enzymes. The understanding of the mutant L‐asparaginases examined in this study will significantly contribute to the development of new and more effective yeast‐derived asparaginases.

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L‐Asparaginase from Lachancea Thermotolerans: Effect of Lys99Ala on Enzyme Performance and in vitro Antileukemic Efficacy

Aktar,

Aysan,

Turunen

et al. 2024

Biotechnology Journal

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Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis

Sundaram,

Kannan,

Chintaluri

et al. 2024

Int Microbiol

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Enzyme Engineering Strategies for the Bioenhancement of l-Asparaginase Used as a Biopharmaceutical

Miranda,

Lefin,

Beltran

et al. 2023

BioDrugs

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Antarctic yeasts as a source of L-asparaginase: Characterization of a glutaminase-activity free L-asparaginase from psychrotolerant yeast Leucosporidium scottii L115

Cited by 4 publications

References 75 publications

L‐Asparaginase from Lachancea Thermotolerans: Effect of Lys99Ala on Enzyme Performance and in vitro Antileukemic Efficacy

L‐Asparaginase from Lachancea Thermotolerans: Effect of Lys99Ala on Enzyme Performance and in vitro Antileukemic Efficacy

Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis

Enzyme Engineering Strategies for the Bioenhancement of l-Asparaginase Used as a Biopharmaceutical

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