Megazyme announces the release of a new, innovative assay procedure for the measuremenet of endo-1,4-b-xylanase.

Measurement of endo-1,4-b-xylanase in industrial enzyme preparations, bread improvers and malted cereal grains

Megazyme is pleased to announce the release of a new, innovative assay procedure for the measuremenet of endo-1,4-b-xylanase (xylanase). The assay is based on hydrolysis of the specific substrate, 4,6-O-(3-ketobutylidene)-4-nitrophenyl-b-45-O-glucosylxylopentaoside as depicted in Scheme 1. On hydrolysis of this substrate, the released 4-nitrophenyl-b-45-O-glucosylxylo-oligosaccharide is immediately hydrolysed by the excess quantities of b-xylosidase present in the substrate mixture, releasing free 4-nitrophenol. The reaction is terminated by addition of alkaline solution with conversion of the 4-nitrophenyl to the yellow, 4-nitrophenolate ion. Increase in yellow colour is directly proportional to the rate of hydrolysis of the xylo-oligosaccharde chain. This assay for xylanase is unique in that it employs a defined, water-soluble substrate in a simple assay format that can be automated. The assay is sensitive, rapid and reproducible and can be applied to any sample containing any xylanase. Megazyme, under the auspices of ICC is planning to run an interlaboratory evaluation of this assay procedure. Are you interested in collaborating? You will be supplied with all required reagents and a set of samples for evaluation.

Please contact Barry McCleary, barryatmegazyme [dot] com.

David Mangan*, Claudio Cornaggia, Agnija Liadova, Niall McCormack, Ruth Ivory,

Vincent A. McKie, Aaron Ormerod, Barry V. McCleary (2017) Novel substrates for the automated and manual assay of endo-1,4-b-xylanase, Carbohydrate Research, 445, 14-22.