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Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis
Enzymatic catalysis in microreactors has attracted growing scientific interest because of high specific surface enabling heat and mass transfer and easier control of reaction parameters in microreactors. However, two major challenges that limit their application are fast inactivation and the inabili...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5487366/ https://www.ncbi.nlm.nih.gov/pubmed/28655888 http://dx.doi.org/10.1038/s41598-017-04216-4 |
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author | Gong, An Zhu, Chang-Tong Xu, Yan Wang, Fang-Qin Tsabing, D’assise Kinfack Wu, Fu-An Wang, Jun |
author_facet | Gong, An Zhu, Chang-Tong Xu, Yan Wang, Fang-Qin Tsabing, D’assise Kinfack Wu, Fu-An Wang, Jun |
author_sort | Gong, An |
collection | PubMed |
description | Enzymatic catalysis in microreactors has attracted growing scientific interest because of high specific surface enabling heat and mass transfer and easier control of reaction parameters in microreactors. However, two major challenges that limit their application are fast inactivation and the inability to the biocatalysts in microchannel reactors. A fluid and unsinkable immobilized enzyme were firstly applied in a microchannel reactor for biocatalysis in this study. Functionalized forms of graphene-immobilized naringinase flowing in microchannels have yielded excellent results for isoquercitrin production. A maximum yield of 92.24 ± 3.26% was obtained after 20 min in a microchannel reactor. Ten cycles of enzymatic hydrolysis reaction were successively completed and an enzyme activity above 85.51 ± 2.76% was maintained. The kinetic parameter V (m)/K (m) increased to 1.9-fold and reaction time was decreased to 1/3 compared with that in a batch reactor. These results indicated that the moving and unsinkable graphene sheets immobilized enzyme with a high persistent specificity and a mild catalytic characteristic enabled the repetitive use of enzyme and significant cost saving for the application of enzyme catalysis. Thus, the developed method has provided an efficient and simple approach for the productive and repeatable microfluidic biocatalysis. |
format | Online Article Text |
id | pubmed-5487366 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-54873662017-06-30 Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis Gong, An Zhu, Chang-Tong Xu, Yan Wang, Fang-Qin Tsabing, D’assise Kinfack Wu, Fu-An Wang, Jun Sci Rep Article Enzymatic catalysis in microreactors has attracted growing scientific interest because of high specific surface enabling heat and mass transfer and easier control of reaction parameters in microreactors. However, two major challenges that limit their application are fast inactivation and the inability to the biocatalysts in microchannel reactors. A fluid and unsinkable immobilized enzyme were firstly applied in a microchannel reactor for biocatalysis in this study. Functionalized forms of graphene-immobilized naringinase flowing in microchannels have yielded excellent results for isoquercitrin production. A maximum yield of 92.24 ± 3.26% was obtained after 20 min in a microchannel reactor. Ten cycles of enzymatic hydrolysis reaction were successively completed and an enzyme activity above 85.51 ± 2.76% was maintained. The kinetic parameter V (m)/K (m) increased to 1.9-fold and reaction time was decreased to 1/3 compared with that in a batch reactor. These results indicated that the moving and unsinkable graphene sheets immobilized enzyme with a high persistent specificity and a mild catalytic characteristic enabled the repetitive use of enzyme and significant cost saving for the application of enzyme catalysis. Thus, the developed method has provided an efficient and simple approach for the productive and repeatable microfluidic biocatalysis. Nature Publishing Group UK 2017-06-27 /pmc/articles/PMC5487366/ /pubmed/28655888 http://dx.doi.org/10.1038/s41598-017-04216-4 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Gong, An Zhu, Chang-Tong Xu, Yan Wang, Fang-Qin Tsabing, D’assise Kinfack Wu, Fu-An Wang, Jun Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis |
title | Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis |
title_full | Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis |
title_fullStr | Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis |
title_full_unstemmed | Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis |
title_short | Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis |
title_sort | moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5487366/ https://www.ncbi.nlm.nih.gov/pubmed/28655888 http://dx.doi.org/10.1038/s41598-017-04216-4 |
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