Title |
A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase)
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Published in |
Analytical & Bioanalytical Chemistry, April 2016
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DOI | 10.1007/s00216-016-9507-y |
Pubmed ID | |
Authors |
David Mangan, Claudio Cornaggia, Vincent McKie, Tadas Kargelis, Barry V. McCleary |
Abstract |
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. Graphical Abstract Principle of the CELLG5 assay. |
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Ireland | 1 | 100% |
Demographic breakdown
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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Unknown | 39 | 100% |
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Researcher | 14 | 36% |
Student > Master | 11 | 28% |
Other | 3 | 8% |
Student > Ph. D. Student | 3 | 8% |
Professor > Associate Professor | 2 | 5% |
Other | 2 | 5% |
Unknown | 4 | 10% |
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Immunology and Microbiology | 1 | 3% |
Other | 1 | 3% |
Unknown | 7 | 18% |