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Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System
The goal of this paper was to develop an in-line immobilized enzyme reactor (IMER) integrated into a capillary electrophoresis platform. In our research, we created the IMER by adsorbing trypsin onto the inner surface of a capillary in a short section. Enzyme immobilization was possible due to the e...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513095/ https://www.ncbi.nlm.nih.gov/pubmed/34641446 http://dx.doi.org/10.3390/molecules26195902 |
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author | Nagy, Cynthia Szabo, Ruben Gaspar, Attila |
author_facet | Nagy, Cynthia Szabo, Ruben Gaspar, Attila |
author_sort | Nagy, Cynthia |
collection | PubMed |
description | The goal of this paper was to develop an in-line immobilized enzyme reactor (IMER) integrated into a capillary electrophoresis platform. In our research, we created the IMER by adsorbing trypsin onto the inner surface of a capillary in a short section. Enzyme immobilization was possible due to the electrostatic attraction between the oppositely charged fused silica capillary surface and trypsin. The reactor was formed by simply injecting and removing trypsin solution from the capillary inlet (~1–2 cms). We investigated the factors affecting the efficiency of the reactor. The main advantages of the proposed method are the fast, cheap, and easy formation of an IMER with in-line protein digestion capability. Human tear samples were used to test the efficiency of the digestion in the microreactor. |
format | Online Article Text |
id | pubmed-8513095 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-85130952021-10-14 Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System Nagy, Cynthia Szabo, Ruben Gaspar, Attila Molecules Article The goal of this paper was to develop an in-line immobilized enzyme reactor (IMER) integrated into a capillary electrophoresis platform. In our research, we created the IMER by adsorbing trypsin onto the inner surface of a capillary in a short section. Enzyme immobilization was possible due to the electrostatic attraction between the oppositely charged fused silica capillary surface and trypsin. The reactor was formed by simply injecting and removing trypsin solution from the capillary inlet (~1–2 cms). We investigated the factors affecting the efficiency of the reactor. The main advantages of the proposed method are the fast, cheap, and easy formation of an IMER with in-line protein digestion capability. Human tear samples were used to test the efficiency of the digestion in the microreactor. MDPI 2021-09-29 /pmc/articles/PMC8513095/ /pubmed/34641446 http://dx.doi.org/10.3390/molecules26195902 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Nagy, Cynthia Szabo, Ruben Gaspar, Attila Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System |
title | Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System |
title_full | Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System |
title_fullStr | Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System |
title_full_unstemmed | Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System |
title_short | Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System |
title_sort | development of an in-line enzyme reactor integrated into a capillary electrophoresis system |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513095/ https://www.ncbi.nlm.nih.gov/pubmed/34641446 http://dx.doi.org/10.3390/molecules26195902 |
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