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

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dc.contributor.authorSánchez-Moguel, Ignacio
dc.contributor.authorCosta-Silva, Tales A.
dc.contributor.authorPillaca-Pullo, Omar S.
dc.contributor.authorFlores-Santos, Juan Carlos
dc.contributor.authorFreire, Rominne Karla Barros
dc.contributor.authorCarretero, Gustavo
dc.contributor.authorda Luz Bueno, Júlia
dc.contributor.authorCamacho-Córdova, David I.
dc.contributor.authorSantos, João H.P.M.
dc.contributor.authorSette, Lara Durães [UNESP]
dc.contributor.authorPessoa-Jr, Adalberto
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidad Privada Norbert Wiener
dc.contributor.institutionAlmirante Paulo Moreira Institute of Studies of the Sea
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionFederal University of ABC
dc.date.accessioned2023-07-29T14:01:05Z
dc.date.available2023-07-29T14:01:05Z
dc.date.issued2023-06-01
dc.description.abstractMicroorganisms 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.en
dc.description.affiliationDepartment of Biochemical and Pharmaceutical Technology School of Pharmaceutical Sciences University of São Paulo, São Paulo
dc.description.affiliationCentro de Investigación en Biodiversidad para la Salud Universidad Privada Norbert Wiener
dc.description.affiliationDepartment of Biochemistry Chemistry Institute University of São Paulo, São Paulo
dc.description.affiliationMarine Biotechnology Division Almirante Paulo Moreira Institute of Studies of the Sea, RJ
dc.description.affiliationDepartment of General and Applied Biology Biosciences Institute São Paulo State University, São Paulo
dc.description.affiliationCenter for Natural and Human Sciences Federal University of ABC, São Paulo
dc.description.affiliationUnespDepartment of General and Applied Biology Biosciences Institute São Paulo State University, São Paulo
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConsejo Nacional de Ciencia y Tecnología
dc.description.sponsorshipIdFAPESP: 2013/08617–7
dc.description.sponsorshipIdFAPESP: 2013/19584–2
dc.description.sponsorshipIdFAPESP: 2019/23620–0
dc.description.sponsorshipIdConsejo Nacional de Ciencia y Tecnología: 298596
dc.format.extent121-132
dc.identifierhttp://dx.doi.org/10.1016/j.procbio.2023.03.003
dc.identifier.citationProcess Biochemistry, v. 129, p. 121-132.
dc.identifier.doi10.1016/j.procbio.2023.03.003
dc.identifier.issn1359-5113
dc.identifier.scopus2-s2.0-85150424621
dc.identifier.urihttp://hdl.handle.net/11449/249053
dc.language.isoeng
dc.relation.ispartofProcess Biochemistry
dc.sourceScopus
dc.subjectAntarctic ecosystems
dc.subjectCold-adapted yeast
dc.subjectL-asparaginase
dc.subjectLeucosporidium scottii
dc.subjectLeukemia
dc.subjectPsychrotolerant yeast
dc.titleAntarctic yeasts as a source of L-asparaginase: Characterization of a glutaminase-activity free L-asparaginase from psychrotolerant yeast Leucosporidium scottii L115en
dc.typeArtigo
unesp.author.orcid0000-0002-7814-9257 0000-0002-7814-9257[2]
unesp.author.orcid0000-0001-7776-6256[6]

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