Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Federal de São Carlos (UFSCar)-
Autor(es): dc.contributorEmpresa Brasileira de Pesquisa Agropecuária (EMBRAPA)-
Autor(es): dc.contributorPNPI RAS Gatchina-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.creatorTonelotto, Mariana-
Autor(es): dc.creatorPirota, Rosangela Donizete Perpetua Buzon-
Autor(es): dc.creatorDelabona, Priscila Da Silva-
Autor(es): dc.creatorBarros, Georgia De Oliveira Figueiredo-
Autor(es): dc.creatorGolubev, Alexander M.-
Autor(es): dc.creatorPolikarpov, Igor-
Autor(es): dc.creatorFarinas, Cristiane Sanchez-
Data de aceite: dc.date.accessioned2022-08-04T22:03:41Z-
Data de disponibilização: dc.date.available2022-08-04T22:03:41Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2014-01-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3109/10242422.2013.801018-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/220044-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/220044-
Descrição: dc.descriptionThe selection of enzyme-producing fungi is useful to obtain enzymes required to hydrolyze lignocellulosic material and thereby contribute to biomass conversion into fuels and chemicals. Besides cellulases, the presence of accessory enzymes in enzyme cocktails is necessary to enhance hydrolysis efficiency. This study evaluates the production, purification, and biochemical-kinetic characterization of β-galactosidase produced by a new strain of Aspergillus niger (P47C3) isolated from the Amazon Forest. The A. niger (P47C3) was cultured under SmF conditions and β-galactosidase was purified in a three-step purification, using an ultrafiltration membrane, ion exchange (TSK-SP), and gel filtration (Sephacryl S-200). The calculated molecular weight of the purified enzyme was 125 kDa. Optimum pH (4.0) and temperature (55°C) of β-galactosidase activity were determined. The values of the kinetic parameters obtained from p-nitrophenyl-β-D- galactopyranoside (PNPG) hydrolysis were 2.2 mM and 0.285 mM/min for Km and Vmax, respectively. The inhibition of PNPG hydrolysis by β-galactosidase in the presence of the inhibitor galactose gave a Ki value of 5.01 mM. As a precursor to elucidating the tertiary structure using X-ray diffraction, the β-galactosidase was crystallized using 0.2 M Tris-HCl buffer, with 12% PEG 4000 as the precipitation agent; the largest crystals were formed at pH 8.6. These results provide the basis for further structural and functional studies of this accessory enzyme to evaluate its potential biotechnological applications. © 2014 Informa UK, Ltd.-
Descrição: dc.descriptionPrograma de Pós-graduação em Biotecnologia Universidade Federal de São Carlos (UFSCar), Rod. Washington Luis, Km 235, 13565-905, São Carlos/SP-
Descrição: dc.descriptionEmbrapa Instrumentação, Rua XV de Novembro, 1452, 13560-970, São Carlos/SP-
Descrição: dc.descriptionPetersburg Nuclear Physics Institute PNPI RAS Gatchina, Leningrad District 188300-
Descrição: dc.descriptionUniversidade do Estado de São Paulo (USP), Av. Trabalhador São-Carlense 400 Arnold Schimidt, 13566-590, São Carlos/SP-
Formato: dc.format13-22-
Idioma: dc.languageen-
Relação: dc.relationBiocatalysis and Biotransformation-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAccessory enzymes-
Palavras-chave: dc.subjectAmazon-
Palavras-chave: dc.subjectAspergillus niger-
Palavras-chave: dc.subjectBiomass-
Palavras-chave: dc.subjectβ-galactosidase-
Título: dc.titleIsolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion-
Tipo de arquivo: dc.typelivro digital-
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