Vmh2 hydrophobin as a tool for the development of "self-immobilizing" enzymes for biosensing.
Biotechnol Bioeng
; 114(1): 46-52, 2017 01.
Article
em En
| MEDLINE
| ID: mdl-27427236
ABSTRACT
Self-assembling proteins forming amyloid fibrils are promising candidates for the fabrication of biomaterials, due to the chemical and mechanical stability of their structures. Among potential applications, their use as platforms for enzyme immobilization is rapidly gathering attention. In this work, we demonstrate that the production of the enzyme glutathione-S-transferase (GST) fused to the class I hydrophobin Vmh2 from Pleurotus ostreatus represents an invaluable tool for the development of self-immobilizing enzymes useful for high throughput analyses. The proposed immobilization strategy is versatile since it can be applied, in principle, to every recombinant protein able to refold from Escherichia coli inclusion bodies. A GST based biosensor has been developed to quantify toxic compounds, such as the pesticides molinate and captan, in aqueous environmental samples. The main advantages of this sensor include simplicity and speed of preparation, high sensitivity, reusability, and accuracy. Biotechnol. Bioeng. 2017;114 46-52. © 2016 Wiley Periodicals, Inc.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Recombinantes de Fusão
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Proteínas Fúngicas
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Técnicas Biossensoriais
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Enzimas Imobilizadas
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Amiloide
Limite:
Animals
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article