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dc.contributor.authorSanchez-Moguel, Ignacio
dc.contributor.authorCosta-Silva, Tales A.
dc.contributor.authorPillaca-Pullo, Omar S.
dc.contributor.authorFlores-Santos, Juan Carlos
dc.contributor.authorBarros Freire, Rominne Karla
dc.contributor.authorCarretero, Gustavo
dc.contributor.authorBueno, Júlia da Luz
dc.contributor.authorCamacho-Cordova, David I.
dc.contributor.authorSantos, Joáo H.P.M.
dc.contributor.authorSette, Lara Duraes
dc.contributor.authorPessoa-Jr., Adalberto
dc.date.accessioned2023-05-23T15:19:37Z
dc.date.available2023-05-23T15:19:37Z
dc.date.issued2023-03-08
dc.identifier.urihttps://hdl.handle.net/20.500.13053/8612
dc.description.abstract“Microorganisms from extreme environments, such as the Antarctic ecosystems, have a great potential to produce enzymes with novel characteristics. Within this context, L-asparaginase (ASNase) obtained from yeast species has been poorly studied. In this study, yeasts isolated from samples collected at Admiralty Bay (King George Island, Antarctica) were tested to produce ASNase. From an initial screening of 40 strains, belonging to 13 different species, Leucosporidium scottii L115 produced an ASNase activity (LsASNase activity: 6.24 U g-1 of dry cell weight) with the lowest glutaminase activity. The LsASNase was purified 227-fold, with a specific activity of 137.01 U mg-1 at 37 ◦C, without glutaminase activity. Moreover, the maximum enzyme activity was observed at pH 7.5 and at a temperature of 55 ◦C. The enzyme is a multimer of 462 kDa, presenting a single band of 53 kDa molecular mass in reduced conditions; after PGNase F treatment, a single band of 45 kDa was observed. The enzymatic kinetic evaluation revealed an allosteric regulation of the enzyme and the kinetic parameters were determined at 37 ◦C, pH 7.0 as substrate affinity constant, K0.5 = 233 μM, kcat = 54.7 s − 1 and Hill coefficient, nH = 1.52, demonstrating positive cooperativity by the enzyme and the substrate. This is the first study to report L. scottii as a source of glutaminase-activity free L-asparaginase, an acute lymphoblastic leukemia drug feature suitable for the treatment of asparagine synthetase negative cancer cells.“es_PE
dc.formatapplication/pdfes_PE
dc.language.isoenges_PE
dc.publisherElsevier Ltdes_PE
dc.rightsinfo:eu-repo/semantics/openAccesses_PE
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/es_PE
dc.subject"L-asparaginase Psychrotolerant yeast Leucosporidium scottii Antarctic ecosystems Cold-adapted yeast Leukemia"es_PE
dc.title“Antarctic yeasts as a source of L-asparaginase: Characterization of a glutaminase-activity free L-asparaginase from psychrotolerant yeast Leucosporidium scottii L115“es_PE
dc.typeinfo:eu-repo/semantics/articlees_PE
dc.identifier.doihttps://doi.org/10.1016/j.procbio.2023.03.003
dc.type.versioninfo:eu-repo/semantics/publishedVersiones_PE
dc.publisher.countryCHes_PE
dc.subject.ocde3.00.00 -- Ciencias médicas, Ciencias de la saludes_PE


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