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Identification of a novel glycoside hydrolase family 8 xylanase from Deinococcus geothermalis and its application at low temperatures
Ist Teil von
Archives of microbiology, 2024-07, Vol.206 (7), p.307-307, Article 307
Ort / Verlag
Berlin/Heidelberg: Springer Berlin Heidelberg
Erscheinungsjahr
2024
Link zum Volltext
Quelle
SpringerLink (Online service)
Beschreibungen/Notizen
Xylanase is the most important hydrolase in the xylan hydrolase system, the main function of which is β-1,4-endo-xylanase, which randomly cleaves xylans to xylo-oligosaccharides and xylose. Xylanase has wide ranging of applications, but there remains little research on the cold-adapted enzymes required in some low-temperature industries. Glycoside hydrolase family 8 (GH8) xylanases have been reported to have cold-adapted enzyme activity. In this study, the xylanase gene
dgeoxyn
was excavated from
Deinococcus geothermalis
through sequence alignment. The recombinant xylanase DgeoXyn encodes 403 amino acids with a theoretical molecular weight of 45.39 kDa. Structural analysis showed that DgeoXyn has a (α/α)6-barrel fold structure typical of GH8 xylanase. At the same time, it has strict substrate specificity, is only active against xylan, and its hydrolysis products include xylobiose, xylotrinose, xytetranose, xylenanose, and a small amount of xylose. DgeoXyn is most active at 70 ℃ and pH 6.0. It is very stable at 10, 20, and 30 ℃, retaining more than 80% of its maximum enzyme activity. The enzyme activity of DgeoXyn increased by 10% after the addition of Mn
2+
and decreased by 80% after the addition of Cu
2+
. The
Km
and
Vmax
of dgeox were 42 mg/ml and 20,000 U/mg, respectively, at a temperature of 70 ℃ and pH of 6.0 using 10 mg/ml beechwood xylan as the substrate. This research on DgeoXyn will provide a theoretical basis for the development and application of low-temperature xylanase.