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A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase)
endo-1,4-β-Glucanase (endo-cellulase, EC 3.2.1.4) is one of the most widely used enzymes in industry. Despite its importance, improved methods for the rapid, selective, quantitative assay of this enzyme have been slow to emerge. In 2014, a novel enzyme-coupled assay that addressed many of the limita...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4873538/ https://www.ncbi.nlm.nih.gov/pubmed/27052773 http://dx.doi.org/10.1007/s00216-016-9507-y |
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author | Mangan, David Cornaggia, Claudio McKie, Vincent Kargelis, Tadas McCleary, Barry V. |
author_facet | Mangan, David Cornaggia, Claudio McKie, Vincent Kargelis, Tadas McCleary, Barry V. |
author_sort | Mangan, David |
collection | PubMed |
description | endo-1,4-β-Glucanase (endo-cellulase, EC 3.2.1.4) is one of the most widely used enzymes in industry. Despite its importance, improved methods for the rapid, selective, quantitative assay of this enzyme have been slow to emerge. In 2014, a novel enzyme-coupled assay that addressed many of the limitations of the existing assay methodology was reported. This involved the use of a bifunctional substrate chemically derived from cellotriose. Reported herein is a much improved version of this assay employing a novel substrate, namely 4,6-O-(3-ketobutylidene)-4-nitrophenyl-β-d-cellopentaoside. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00216-016-9507-y) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4873538 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-48735382016-06-21 A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) Mangan, David Cornaggia, Claudio McKie, Vincent Kargelis, Tadas McCleary, Barry V. Anal Bioanal Chem Research Paper endo-1,4-β-Glucanase (endo-cellulase, EC 3.2.1.4) is one of the most widely used enzymes in industry. Despite its importance, improved methods for the rapid, selective, quantitative assay of this enzyme have been slow to emerge. In 2014, a novel enzyme-coupled assay that addressed many of the limitations of the existing assay methodology was reported. This involved the use of a bifunctional substrate chemically derived from cellotriose. Reported herein is a much improved version of this assay employing a novel substrate, namely 4,6-O-(3-ketobutylidene)-4-nitrophenyl-β-d-cellopentaoside. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00216-016-9507-y) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2016-04-06 2016 /pmc/articles/PMC4873538/ /pubmed/27052773 http://dx.doi.org/10.1007/s00216-016-9507-y Text en © Springer-Verlag Berlin Heidelberg 2016 |
spellingShingle | Research Paper Mangan, David Cornaggia, Claudio McKie, Vincent Kargelis, Tadas McCleary, Barry V. A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) |
title | A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) |
title_full | A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) |
title_fullStr | A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) |
title_full_unstemmed | A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) |
title_short | A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) |
title_sort | novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase) |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4873538/ https://www.ncbi.nlm.nih.gov/pubmed/27052773 http://dx.doi.org/10.1007/s00216-016-9507-y |
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