3.125 mL; 5,000 Units
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|Content:||3.125 mL; 5,000 Units|
|Formulation:||In 3.2 M ammonium sulphate|
|Stability:||> 4 years at 4oC|
|Synonyms:||endo-1,4-beta-xylanase; 4-beta-D-xylan xylanohydrolase|
|Concentration:||Supplied at ~ 1,600 U/mL|
|Expression:||Purified from Aspergillus aculeatus|
|Specificity:||endo-hydrolysis of (1,4)-β-D-xylosidic linkages in xylans.|
|Specific Activity:||~ 30 U/mg (40oC, pH 4.5 on wheat arabinoxylan)|
|Unit Definition:||One Unit of xylanase activity is defined as the amount of enzyme required to release one µmole of xylose reducing-sugar equivalents from wheat arabinoxylan per minute under the conditions stated.|
|Application examples:||For use in research.|
High purity endo-1,4-β-Xylanase (Aspergillus aculeatus) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
View all of our Carbohydrate Active enZYme products.
(Trichoderma longibrachiatum) E-XYAN4 - endo-1,4-β-Xylanase M4 (Aspergillus niger) E-XYRU6 - endo-1,4-β-Xylanase (rumen microorganism) E-XYNAP - endo-1,4-β-Xylanase (Aeromonas punctata) E-XYNBS - endo-1,4-β-Xylanase
(Bacillus stearothermophilus T6) E-XYNACJ - endo-1,4-β-Xylanase (Cellvibrio japonicus) E-XYNBCM - endo-1,4-β-Xylanase (Cellvibrio mixtus) E-XYLNP - endo-1,4-β-Xylanase (Neocallimastix patriciarum) E-XYLATM - endo-1,4-β-Xylanase (Thermotoga maritima)
Mangan, D., Cornaggia, C., Liadova, A., McCormack, N., Ivory, R., McKie, V. A., Ormerod, A. & McCleary, D. V. (2017). Carbohydrate Research, 445, 14-22.
endo-1,4-β-Xylanase (EC 126.96.36.199) 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 XylX6 assay, that employs a novel substrate, namely 4,6-O-(3-ketobutylidene)-4-nitrophenyl-β-45-O-glucosyl-xylopentaoside. The development of the substrate and associated assay is discussed here and the relationship between the activity values obtained with the XylX6 assay versus traditional reducing sugar assays and its specificity and reproducibility were thoroughly investigated.Hide Abstract