Heterologous expression, purification and biochemical characterization of a new xylanase from Myceliophthora heterothallica F.2.1.4

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorde Amo, Gabriela Salvador-
Autor(es): dc.creatorBezerra-Bussoli, Carolina-
Autor(es): dc.creatorda Silva, Ronivaldo Rodrigues-
Autor(es): dc.creatorKishi, Luciano Takeshi-
Autor(es): dc.creatorFerreira, Henrique-
Autor(es): dc.creatorMariutti, Ricardo Barros-
Autor(es): dc.creatorArni, Raghuvir Krishnaswamy-
Autor(es): dc.creatorGomes, Eleni-
Autor(es): dc.creatorBonilla-Rodriguez, Gustavo Orlando-
Data de aceite: dc.date.accessioned2021-03-11T01:37:04Z-
Data de disponibilização: dc.date.available2021-03-11T01:37:04Z-
Data de envio: dc.date.issued2019-10-06-
Data de envio: dc.date.issued2019-10-06-
Data de envio: dc.date.issued2019-06-15-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2019.03.108-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/188864-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/188864-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionFinanciadora de Estudos e Projetos-
Descrição: dc.descriptionMyceliophthora heterothallica is a thermophilic fungus potentially relevant for the production of enzymes involved in the degradation of plant biomass. A xylanase encoding gene of this species was identified by means of RT-PCR using primers designed based on a xylanase coding sequence (GH11) of the fungus M. thermophila. The obtained gene was ligated to the vector pET28a(+) and the construct was transformed into Escherichia coli cells. The recombinant xylanase (r-ec-XylMh) was heterologously expressed, and the highest activity was observed at 55 °C and pH 6. The enzyme stability was greater than 70% between pH 4.5 and 9.5 and the inclusion of glycerol (50%) resulted in a significant increase in thermostability. Under these conditions, the enzyme retained more than 50% residual activity when incubated at 65 °C for 1 h, and approximately 30% activity when incubated at 70 °C for the same period. The tested cations did not increase xylanolytic activity, and the enzyme indicated significant tolerance to several phenolic compounds after 24 h, as well as high specificity for xylan, with no activity for other substrates such as CMC (carboxymethylcellulose), Avicel, pNPX (p-nitrophenyl-β-D-xylopyranoside) and pNPA (p-nitrophenyl-α-L-arabinofuranoside), and is thus, of potential relevance in pulp bleaching.-
Formato: dc.format798-805-
Idioma: dc.languageen-
Relação: dc.relationInternational Journal of Biological Macromolecules-
Direitos: dc.rightsopenAccess-
Palavras-chave: dc.subjectHeterologous expression-
Palavras-chave: dc.subjectMyceliophthora heterothallica-
Palavras-chave: dc.subjectRecombinant xylanase-
Palavras-chave: dc.subjectReverse transcriptase PCR-
Palavras-chave: dc.subjectThermophilic fungus-
Título: dc.titleHeterologous expression, purification and biochemical characterization of a new xylanase from Myceliophthora heterothallica F.2.1.4-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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