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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...

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Autores principales: Mangan, David, Cornaggia, Claudio, McKie, Vincent, Kargelis, Tadas, McCleary, Barry V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2016
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.
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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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