Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase)

McCleary, Barry V.; Mangan, David; Daly, Robin M.; Fort, Sébastien; Ivory, Ruth; McCormack, Niall

doi:10.1016/j.carres.2013.12.001

Cited by 24 publications

(15 citation statements)

References 19 publications

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“…They have a low degree of polymerization (DP) typically lower than 10 and are thus easier to process and characterize compared to the insoluble native cellulose. Their potential applications can be as cellulose models as they conserve their inherent structure or as substrates for the assessment of cellulase activity for example . Also, as they are not digested by the human organism, they can be used for their prebiotic status as dietary fibre, sweetener or weight controlling agent .…”

Section: Introductionmentioning

confidence: 99%

Water-soluble cellulose oligomer production by chemical and enzymatic synthesis: a mini-review

et al. 2017

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This mini‐review focuses on the production of water‐soluble cellulose oligomers. They are easier to handle than cellulose while still having some very interesting cellulose features. Their production is not trivial and they are thus seldom commercially available or are available at high prices and only in small quantities (100 mg or less). The goal of this mini‐review is to describe various routes to obtain these cellulose oligomers. Several examples of chemical or enzymatic synthesis and enzymatic or acidic depolymerization are presented. All the pathways considered are then compared according to several criteria: polymerization degree, yield, availability and cost of reagents, reaction time, etc. As most of the pathways produce a mixture of cellulose oligomers, techniques to separate them according to their length are also discussed. © 2017 Society of Chemical Industry

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Section: Introductionmentioning

confidence: 99%

Water-soluble cellulose oligomer production by chemical and enzymatic synthesis: a mini-review

et al. 2017

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“…This issue can be resolved with a straightforward pre-incubation with AMG that will be discussed in depth later in this section. An alternative approach to the measurement of LD is to employ end-blocked colourimetric or fluorimetric substrates using a similar approach to that reported for the measurement of aamylase (McCleary and Sheehan, 1987;McCleary et al, 2002), cellulase (McCleary et al, 2014a) and pullulanase (McCleary et al, 2014b). A recent publication (Bøjstrup et al, 2014) describes the use of an unblocked substrate, namely 2-chloro-4-nitrophenyl-b-6 3 -a-D-glucosyl-maltotriosyl-maltotrioside, for the assay of pullulanase and limit-dextrinase.…”

Section: Resultsmentioning

confidence: 96%

Colourimetric and fluorimetric substrates for the assay of limit dextrinase

Mangan¹,

McCleary²,

Cornaggia³

et al. 2015

Journal of Cereal Science

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“…4,6- O -Benzylidene-2-chloro-4-nitrophenyl-β- d -cellopentaoside ( 3 ) and 4,6- O -benzylidene-2-chloro-4-nitrophenyl-β- d -cellohexaoside ( 4 ) were synthesized from the corresponding cellooligosaccharides using previously described synthetic methodology [ 18 , 20 ].…”

Section: Methodsmentioning

confidence: 99%

“…Recently, a coupled enzyme activity assay for EG was reported employing 4,6- O -benzylidene-2-chloro-4-nitrophenyl-β- d -cellotrioside ( 1 ) [ 18 ]. The analogous fluorimetric assay employing 4,6- O -benzylidene-4-methylumbelliferyl-β- d -cellotrioside allowing improved sensitivity ( 2 ) was reported soon after [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

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

Mangan¹,

Cornaggia²,

McKie³

et al. 2016

Anal Bioanal Chem

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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.

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Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase)

Cited by 24 publications

References 19 publications

Water-soluble cellulose oligomer production by chemical and enzymatic synthesis: a mini-review

Water-soluble cellulose oligomer production by chemical and enzymatic synthesis: a mini-review

Colourimetric and fluorimetric substrates for the assay of limit dextrinase

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

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