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MDL number:

biological source

wood (beech wood)




4-O-Methyl-D-glucurono-D-xylan has been used in a study to assess ecto-glycanases and metabolic stability of the capsule in Cryptococcus neoformans. It has also been used in a study that investigated soluble chromogenic substrates for the assay of xylanases and glucanases.

Storage Class Code

13 - Non Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

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Certificate of Origin

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Danka Maceková et al.
Journal of basic microbiology, 46(6), 470-479 (2006-12-02)
We have identified a number of ecto-glycanases (glycosylhydrolases) associated with the capsule and/or the cell wall of Cryptococcus neoformans. The enzyme activities detected included alpha-mannosidase, alpha-, and beta -glucosidase, alpha-, and beta-galactosidase, beta-xylosidase, beta-glucuronidase, and endo-beta-1,3-glucanase. Small portions of the
P Biely et al.
Analytical biochemistry, 144(1), 142-146 (1985-01-01)
New soluble chromogenic substrates were prepared for specific and rapid assays of endo-1,4-beta-xylanases and endo-1,4-beta-glucanases. A soluble beechwood 4-O-methyl-D-glucurono-D-xylan was dyed with Remazol brilliant blue R, and hydroxyethylcellulose was coupled to Ostazin brilliant red H-3B. The assays are based on
Thu V Vuong et al.
Biotechnology for biofuels, 13, 51-51 (2020-03-20)
Dicarboxylic acids offer several applications in detergent builder and biopolymer fields. One of these acids, 4-O-methyl d-glucaric acid, could potentially be produced from glucuronoxylans, which are a comparatively underused fraction of wood and agricultural biorefineries. Accordingly, an enzymatic pathway was
Junpei Zhou et al.
Folia microbiologica, 59(5), 423-431 (2014-04-15)
A glycosyl hydrolase family 10 endoxylanase from Bacillus sp. HJ14 was grouped in a separated cluster with another six Bacillus endoxylanases which have not been characterized. These Bacillus endoxylanases showed less than 52% amino acid sequence identity with other endoxylanases

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