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

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Do Centro-Oeste-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorRatuchne, Aline-
Autor(es): dc.creatorIzidoro, Simone Cristine-
Autor(es): dc.creatorBeitel, Susan Michelz-
Autor(es): dc.creatorLacerda, Lorena Tigre-
Autor(es): dc.creatorKnob, Adriana-
Data de aceite: dc.date.accessioned2025-08-21T22:13:07Z-
Data de disponibilização: dc.date.available2025-08-21T22:13:07Z-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-06-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1007/s42770-023-00939-x-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/246988-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/246988-
Descrição: dc.descriptionl-Asparaginase (l-ASNase) is a potent chemotherapeutic drug employed to treat leukemia and lymphoma. Currently, l-ASNases for therapeutic use are obtained from Escherichia coli and Dickeya chrysanthemi (Erwinia chrysanthemi). Despite their therapeutic potential, enzymes from bacteria are subject to inducing immune responses, resulting in a higher number of side effects. Eukaryote producers, such as fungi, may provide therapeutic alternatives through enzymes that induce relatively less toxicity and immune responses. Additional expected benefits from yeast-derived enzymes include higher activity and stability in physiological conditions. This work describes the new potential therapeutic candidate l-ASNase from the yeast Meyerozyma guilliermondii. A statistical approach (full factorial central composite design) was used to optimize l-ASNase production, considering l-asparagine and glucose concentration, pH of the medium, and cultivation time as independent factors. In addition, the crude enzymes were biochemically characterized, in terms of temperature and optimal pH, thermostability, pH stability, and associated glutaminase or urease activities. Our results showed that enzyme production increased after supplementing a pH 4.0 medium with 1.0% l-asparagine and 0.5% glucose during 75 h of cultivation. Under these optimized conditions, l-ASNase production reached 26.01 U mL−1, which is suitable for scale-up studies. The produced l-ASNase exhibits maximal activity at 37 °C and pH 7.0 and is highly stable under physiological conditions. In addition, M. guilliermondiil-ASNase has no associated glutaminase or urease activities, demonstrating its potential as a promising antineoplastic agent.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionDepartamento de Ciências Biológicas Universidade Estadual Do Centro-Oeste, Camargo Varela de Sá Street, 03, Paraná State-
Descrição: dc.descriptionDepartamento de Biologia Geral E Aplicada Universidade Estadual Paulista (UNESP), 24A Avenue, 1515, São Paulo State-
Descrição: dc.descriptionDepartamento de Biologia Geral E Aplicada Universidade Estadual Paulista (UNESP), 24A Avenue, 1515, São Paulo State-
Descrição: dc.descriptionCAPES: Finance code 001-
Descrição: dc.descriptionCNPq: Grant. 443953/2014-7-
Formato: dc.format715-723-
Idioma: dc.languageen-
Relação: dc.relationBrazilian Journal of Microbiology-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectBiochemical properties-
Palavras-chave: dc.subjectOptimization-
Palavras-chave: dc.subjectTherapeutic enzymes-
Palavras-chave: dc.subjectYeasts-
Título: dc.titleA new extracellular glutaminase and urease-free l-asparaginase from Meyerozyma guilliermondii-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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