Novel substrates for the automated and manual assay of endo-1,4-β-xylanase

被引：14

作者：

Mangan, David ^{[1
]}

Cornaggia, Claudio ^{[1
]}

Liadova, Agnija ^{[1
]}

McCormack, Niall ^{[1
]}

Ivory, Ruth ^{[1
]}

McKie, Vincent A. ^{[1
]}

Ormerod, Aaron ^{[1
]}

McCleary, Barry V. ^{[1
]}

机构：

[1] Megazyme, IDA Business Pk,Southern Cross Rd, Bray, Co Wicklow, Ireland

来源：

CARBOHYDRATE RESEARCH | 2017年 / 445卷

关键词：

ALPHA-AMYLASE; ENZYMATIC-SYNTHESIS; STRUCTURAL BASIS; BETA-XYLOSIDASE; DAMAGED WHEAT; XYLANASE; ENDO-1,4-BETA-GLUCANASE; CELLULASE; OLIGOSACCHARIDES;

D O I：

10.1016/j.carres.2017.02.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

endo-1,4-beta-Xylanase (EC 3.2.1.8) is employed across a broad range of industries including animal feed, brewing, baking, biofuels, detergents and pulp (paper). Despite its importance, a rapid, reliable, reproducible, automatable assay for this enzyme that is based on the use of a chemically defined substrate has not been described to date. Reported herein is a new enzyme coupled assay procedure, termed the Xy1X6 assay, that employs a novel substrate, namely 4,6-O-(3-ketobutylidene)-4-nitropheny1-beta-4(5)-O-glucosyl-xylopentaoside. The development of the substrate and associated assay is discussed here and the relationship between the activity values obtained with the Xy1X6 assay versus traditional reducing sugar assays and its specificity and reproducibility were thoroughly investigated. (C) 2017 Elsevier Ltd. All rights reserved.

引用

页码：14 / 22

页数：9

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