V900513
Xylan
Vetec™, reagent grade, 90%
Synonym(s):
Poly(β-D-xylopyranose[1→4])
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About This Item
UNSPSC Code:
12352201
MDL number:
grade
reagent grade
product line
Vetec™
assay
90%
form
powder
mp
300 °C
Other Notes
To gain a comprehensive understanding of our extensive range of Polysaccharides for your research, we encourage you to visit our Carbohydrates Category page.
Legal Information
Vetec is a trademark of Merck KGaA, Darmstadt, Germany
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Changjie Bao et al.
Scientific reports, 10(1), 11686-11686 (2020-07-17)
Saccharomyces cerevisiae-based expression systems, which rely on safe, food-grade strains, are low cost, simple to operate, and can be used for large-scale fermentation. However, low levels of foreign protein expression by S. cerevisiae have limited their widespread application. The ability
Masashi Kiyohara et al.
Journal of biochemistry, 140(3), 369-373 (2006-08-08)
Recently we reported the molecular cloning and characterization of a novel beta-1,3-xylanase from the marine bacterium Vibrio sp. AX-4 [Kiyohara et al. (2005) Biochem. J. 388, 949-957]. We report here the structural analysis of oligosaccharides generated from beta-1,3-xylan of a
Hiroshi Hashimoto et al.
FEBS letters, 579(20), 4324-4328 (2005-08-03)
Here, we present the crystal structure of the family 31 carbohydrate-binding module (CBM) of beta-1,3-xylanase from Alcaligenes sp. strain XY-234 (AlcCBM31) determined at a resolution of 1.25A. The AlcCBM31 shows affinity with only beta-1,3-xylan. The AlcCBM31 molecule makes a beta-sandwich
Masashi Kiyohara et al.
Journal of biochemistry, 146(5), 633-641 (2009-07-17)
beta-1,3-Xylanase from Vibrio sp. strain AX-4 (XYL4) is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules (CBMs) belonging to family 31 in the C-terminal region. To investigate the
I Yamaura et al.
Agricultural and biological chemistry, 54(4), 921-926 (1990-04-01)
An endo-1,3-beta-D-xylanase (1,3-beta-D-xylan xylanohydrolase, EC 3.2.1.32) was purified from the culture fluid of Pseudomonas sp. PT-5 by ammonium sulfate fractionation, DEAE-Sepharose CL-6B, Toyopearl HW-50S, and Butyl-Toyopearl 650 M column chromatography. The purified enzyme gave a single band on polyacrylamide gel
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