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Enzyme Immobilization on Nanoporous Gold: A Review

Nanoporous gold (referred to as np-Au or NPG) has emerged over the past 10 years as a new support for enzyme immobilization. The material has appealing features of ease of preparation, tunability of pore size, high surface to volume ratio, and compatibility with multiple strategies for enzyme immobi...

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Autor principal: Stine, Keith J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE Publications 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751899/
https://www.ncbi.nlm.nih.gov/pubmed/29308011
http://dx.doi.org/10.1177/1178626417748607
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author Stine, Keith J
author_facet Stine, Keith J
author_sort Stine, Keith J
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description Nanoporous gold (referred to as np-Au or NPG) has emerged over the past 10 years as a new support for enzyme immobilization. The material has appealing features of ease of preparation, tunability of pore size, high surface to volume ratio, and compatibility with multiple strategies for enzyme immobilization. The np-Au material is especially of interest for immobilization of redox enzymes for biosensor and biofuel cell applications given the ability to construct electrodes of high surface area and stability. Adjustment of the pore size of np-Au can yield enhancements in enzyme thermal stability. Glucose oxidase immobilization on np-Au has been a focus for development of glucose sensors. Immobilization of laccase and related enzymes has demonstrated the utility of np-Au for construction of biofuel cells. Np-Au has been used to immobilize other redox enzymes, enzyme conjugates for use in bioassays, and enzymes of interest for industrial processes.
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spelling pubmed-57518992018-01-05 Enzyme Immobilization on Nanoporous Gold: A Review Stine, Keith J Biochem Insights Review Nanoporous gold (referred to as np-Au or NPG) has emerged over the past 10 years as a new support for enzyme immobilization. The material has appealing features of ease of preparation, tunability of pore size, high surface to volume ratio, and compatibility with multiple strategies for enzyme immobilization. The np-Au material is especially of interest for immobilization of redox enzymes for biosensor and biofuel cell applications given the ability to construct electrodes of high surface area and stability. Adjustment of the pore size of np-Au can yield enhancements in enzyme thermal stability. Glucose oxidase immobilization on np-Au has been a focus for development of glucose sensors. Immobilization of laccase and related enzymes has demonstrated the utility of np-Au for construction of biofuel cells. Np-Au has been used to immobilize other redox enzymes, enzyme conjugates for use in bioassays, and enzymes of interest for industrial processes. SAGE Publications 2017-12-17 /pmc/articles/PMC5751899/ /pubmed/29308011 http://dx.doi.org/10.1177/1178626417748607 Text en © The Author(s) 2017 http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution 4.0 License (http://www.creativecommons.org/licenses/by/4.0/) which permits any use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage).
spellingShingle Review
Stine, Keith J
Enzyme Immobilization on Nanoporous Gold: A Review
title Enzyme Immobilization on Nanoporous Gold: A Review
title_full Enzyme Immobilization on Nanoporous Gold: A Review
title_fullStr Enzyme Immobilization on Nanoporous Gold: A Review
title_full_unstemmed Enzyme Immobilization on Nanoporous Gold: A Review
title_short Enzyme Immobilization on Nanoporous Gold: A Review
title_sort enzyme immobilization on nanoporous gold: a review
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751899/
https://www.ncbi.nlm.nih.gov/pubmed/29308011
http://dx.doi.org/10.1177/1178626417748607
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