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Screening of Supports for the Immobilization of β-Glucosidase

A set of supports were screened for the immobilization of a partially purified extract of β-glucosidase from Aspergillus sp. These supports, namely, Eupergit, Amberlite, alginate, gelatin, polyvinyl alcohol- (PVA-) based matrices (Lentikats), and sol-gel, have proved effective for the implementation...

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Detalles Bibliográficos
Autores principales: Figueira, Joelise de Alencar, Dias, Fernanda Furlan Gonçalves, Sato, Hélia Harumi, Fernandes, Pedro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE-Hindawi Access to Research 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3170910/
https://www.ncbi.nlm.nih.gov/pubmed/21915374
http://dx.doi.org/10.4061/2011/642460
Descripción
Sumario:A set of supports were screened for the immobilization of a partially purified extract of β-glucosidase from Aspergillus sp. These supports, namely, Eupergit, Amberlite, alginate, gelatin, polyvinyl alcohol- (PVA-) based matrices (Lentikats), and sol-gel, have proved effective for the implementation of some other enzyme-based processes. The initial criterion for selection of promising supports prior to further characterization relied on the retention of the catalytic activity following immobilization. Based on such criterion, where immobilization in sol-gel and in Lentikats outmatched the remaining approaches, those two systems were further characterized. Immobilization did not alter the pH/activity profile, whereas the temperature/activity profile was improved when sol-gel support was assayed. Both thermal and pH stability were improved as a result of immobilization. An increase in the apparent K (M) (Michaelis constant) was observed following immobilization, suggesting diffusion limitations.