A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase).

Content Provider	Europe PMC
Author	Mangan, David Cornaggia, Claudio McKie, Vincent Kargelis, Tadas McCleary, Barry V.
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 AbstractPrinciple of the CELLG5 assayElectronic supplementary materialThe online version of this article (doi:10.1007/s00216-016-9507-y) contains supplementary material, which is available to authorized users.
ISSN	16182642
Journal	Analytical and Bioanalytical Chemistry
Volume Number	408
PubMed Central reference number	PMC4873538
Issue Number	15
PubMed reference number	27052773
e-ISSN	16182650
DOI	10.1007/s00216-016-9507-y
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2016-04-06
Publisher Place	Berlin/Heidelberg
Access Restriction	Open
Rights License	© Springer-Verlag Berlin Heidelberg 2016
Subject Keyword	endo-1,4-β-Glucanase Cellulase Assay Colorimetric CELLG5 Automation
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Biochemistry