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dc.creatorMól, Paula Chequer Gouveia-
dc.creatorVeríssimo, Lizzy Ayra Alcântara-
dc.creatorMinim, Luis Antonio-
dc.creatorSilva, Roberto da-
dc.date.accessioned2022-08-18T16:53:02Z-
dc.date.available2022-08-18T16:53:02Z-
dc.date.issued2022-06-
dc.identifier.citationMÓL, P. C. G. et al. Adsorption and immobilization of b-glucosidase fromThermoascus aurantiacus on macroporous cryogel by hydrophobic interaction. Preparative Biochemistry & Biotechnology, [S.l.], June 2022. DOI: 10.1080/10826068.2022.2081860.pt_BR
dc.identifier.urihttps://www.tandfonline.com/doi/abs/10.1080/10826068.2022.2081860pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/53309-
dc.description.abstractEnzyme 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.pt_BR
dc.languageen_USpt_BR
dc.publisherTaylor & Francispt_BR
dc.rightsrestrictAccesspt_BR
dc.sourcePreparative Biochemistry & Biotechnologypt_BR
dc.subjectAdsorptionpt_BR
dc.subjectβ-glucosidasept_BR
dc.subjectCryogelpt_BR
dc.subjectHydrophobic interactionpt_BR
dc.subjectL-phenylalaninept_BR
dc.titleAdsorption and immobilization of b-glucosidase fromThermoascus aurantiacus on macroporous cryogel by hydrophobic interactionpt_BR
dc.typeArtigopt_BR
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