Multimerization of an Alcohol Dehydrogenase by Fusion to a Designed Self-Assembling Protein Results in Enhanced Bioelectrocatalytic Operational Stability.
ACS Appl Mater Interfaces
; 11(22): 20022-20028, 2019 Jun 05.
Article
em En
| MEDLINE
| ID: mdl-31066271
ABSTRACT
Proteins designed for supramolecular assembly provide a simple means to immobilize and organize enzymes for biotechnology applications. We have genetically fused the thermostable alcohol dehydrogenase D (AdhD) from Pyrococcus furiosus to a computationally designed cage-forming protein (O3-33). The trimeric form of the O3-33-AdhD fusion protein was most active in solution. The immobilization of the fusion protein on bioelectrodes leads to a doubling of the electrochemical operational stability as compared to the unfused control proteins. Thus, the fusion of enzymes to the designed self-assembling domains offers a simple strategy to increase the stability in biocatalytic systems.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Álcool Desidrogenase
/
Enzimas Imobilizadas
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article