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X0627

Sigma-Aldrich

Xylan from oat spelts

Xylose ≥70 % by HPAE (after hydrolysis)

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Synonym(s):
Poly(β-D-xylopyranose[1→4])
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352201

composition

arabinose, ≤10% HPAE
glucose, ≤15% HPAE
Xylose, ≥70% HPAE (after hydrolysis)

solubility

1 M NaOH: may be turbid

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WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Cedric Montanier et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(9), 3065-3070 (2009-02-17)
Enzymes that hydrolyze complex carbohydrates play important roles in numerous biological processes that result in the maintenance of marine and terrestrial life. These enzymes often contain noncatalytic carbohydrate binding modules (CBMs) that have important substrate-targeting functions. In general, there is
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, 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
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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