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


ABSTRACT: endo-1,4-?-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-?-D-cellopentaoside. Graphical Abstract Principle of the CELLG5 assay.

SUBMITTER: Mangan D 

PROVIDER: S-EPMC4873538 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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

Mangan David D   Cornaggia Claudio C   McKie Vincent V   Kargelis Tadas T   McCleary Barry V BV  

Analytical and bioanalytical chemistry 20160406 15


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 em  ...[more]

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