|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 ~ 1,300 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 18.104.22.168) 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
Characterization of an acetyl xylan esterase from the marine bacterium Ochrovirga pacifica and its synergism with xylanase on beechwood xylan.
Hettiarachchi, S. A., Kwon, Y. K., Lee, Y., Jo, E., Eom, T. Y., Kang, Y. H., Zoysa, M. D., Marasinghe, S. D. & Oh, C. (2019). Microbial Cell Factories, 18(1), 122.
Background: Acetyl xylan esterase plays an important role in the complete enzymatic hydrolysis of lignocellulosic materials. It hydrolyzes the ester linkages of acetic acid in xylan and supports and enhances the activity of xylanase. This study was conducted to identify and overexpress the acetyl xylan esterase (AXE) gene revealed by the genomic sequencing of the marine bacterium Ochrovirga pacifica. Results: The AXE gene has an 864-bp open reading frame that encodes 287 aa and consists of an AXE domain from aa 60 to 274. Gene was cloned to pET-16b vector and expressed the recombinant AXE (rAXE) in Escherichia coli BL21 (DE3). The predicted molecular mass was 31.75 kDa. The maximum specific activity (40.08 U/mg) was recorded at the optimal temperature and pH which were 50°C and pH 8.0, respectively. The thermal stability assay showed that AXE maintains its residual activity almost constantly throughout and after incubation at 45°C for 120 min. The synergism of AXE with xylanase on beechwood xylan, increased the relative activity 1.41-fold. Conclusion: Resulted higher relative activity of rAXE with commercially available xylanase on beechwood xylan showed its potential for the use of rAXE in industrial purposes as a de-esterification enzyme to hydrolyze xylan and hemicellulose-like complex substrates.Hide Abstract