M5144
4-O-Methyl-D-glucurono-D-xylan
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About This Item
UNSPSC Code:
12352201
MDL number:
biological source
wood (beech wood)
form
powder
Application
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.
Other Notes
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Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
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
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
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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