Adsorption and immobilization of β-glucosidase from Thermoascus aurantiacus on macroporous cryogel by hydrophobic interaction

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorFederal University of Lavras-
Autor(es): dc.contributorFederal University of Viçosa-
Autor(es): dc.creatorMól, Paula Chequer Gouveia-
Autor(es): dc.creatorVeríssimo, Lizzy Ayra Alcântara-
Autor(es): dc.creatorMinim, Luis Antonio-
Autor(es): dc.creatorSilva, Roberto da-
Data de aceite: dc.date.accessioned2025-08-21T15:23:37Z-
Data de disponibilização: dc.date.available2025-08-21T15:23:37Z-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2021-12-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1080/10826068.2022.2081860-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/240209-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/240209-
Descrição: dc.descriptionEnzyme immobilization has been reported as a promising approach to improving parameters such as thermal stability, pH and reusability. In this study, a polyacrylamide cryogel functionalized with L-phenylalanine was prepared to be used in the adsorption of β-glucosidase from Thermoascus aurantiacus, aiming at its separation and also its immobilization on the cryogel matrix. The enzyme was produced by solid state fermentation. First, the adsorption was studied as a function of the pH and the resulting yield (Y, %) and purification factor (PF, dimensionless) were determined (1.57–5.13 and 64.19–91.20, respectively). The PF and yield from eluate samples obtained at pH 3.0 were the highest (5.13 and 91.20, respectively). Then, β-glucosidase was immobilized on the hydrophobic cryogel and the recovery activities (%) were determined as a function of temperature and in the presence of different saline solutions. The values ranged from 14.45 to 45.97. As expected, salt type and ionic strength affected the activity remained in the immobilized β-glucosidase. The average bioreactor activity was 39.9 U/g of dry cryogel and its operational stability was measured, with no decrease in activity being observed during seven cycles. Kinetic parameters of free and immobilized enzyme were determined according to different models.-
Descrição: dc.descriptionLaboratory of Biochemistry and Applied Microbiology UNESP–São Paulo State University, SP-
Descrição: dc.descriptionDepartment of Food Science Federal University of Lavras, MG-
Descrição: dc.descriptionDepartment of Food Technology Federal University of Viçosa, MG-
Descrição: dc.descriptionLaboratory of Biochemistry and Applied Microbiology UNESP–São Paulo State University, SP-
Idioma: dc.languageen-
Relação: dc.relationPreparative Biochemistry and Biotechnology-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAdsorption-
Palavras-chave: dc.subjectcryogel-
Palavras-chave: dc.subjecthydrophobic interaction-
Palavras-chave: dc.subjectL-phenylalanine-
Palavras-chave: dc.subjectβ-glucosidase-
Título: dc.titleAdsorption and immobilization of β-glucosidase from Thermoascus aurantiacus on macroporous cryogel by hydrophobic interaction-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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