Abstract
The activity of novel uncharacterized extremophilic L-asparaginases from the psychrophilic fungi Sclerotinia borealis, the thermoacidophilic crenarchea Acidilobus saccharovorans, and the thermophilic bacteria Melioribacter roseus were studied. Active enzymes were produced via the expression of the native L-asparaginase gene from M. roseus (MrA) and synthetic genes encoding fungal S. borealis (SbA) and archeal A. saccharovorans (AsA) L-asparaginases after codon optimization in Escherichia coli cells. In the study, the maximum specific activity at different temperatures and pH was observed for MrA. The activity of MrA crude extract was highest at 75°С and a pH of 9.0. Metal ions (1 mM) differed in their effects on enzyme activity. Сu2+ and Zn2+ ions completely abolished enzyme activity. Changes in the specific activity of MrA crude extract in the presence of Fe3+, Ni2+, Ca2+, and Mg2+ varied within 5–28%. Our findings show that L-asparaginase of M. roseus may be a promising object for the further study of enzymatic properties and biotechnological applications.
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The work was partially supported by the Russian Foundation for Basic Research, project no. 19-08-01112, and by the Program for Basic Scientific Research in the Russian Federation for a long-term period (2021–2030).
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The authors declare that they have no conflict of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.
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This article is dedicated to the memory of M. A. El’darov
Translated by E. V. Makeeva
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Dumina, M.V., Zhgun, A.A., Pokrovskay, M.V. et al. Comparison of Enzymatic Activity of Novel Recombinant L-asparaginases of Extremophiles. Appl Biochem Microbiol 57, 594–602 (2021). https://doi.org/10.1134/S0003683821050057
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DOI: https://doi.org/10.1134/S0003683821050057