ArticleJournal of microbiology (Seoul, Korea)2010
The role of carbohydrate-binding module (CBM) repeat of a multimodular xylanase (XynX) from Clostridium thermocellum in cellulose and xylan binding.
Article in Journal of microbiology (Seoul, Korea), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 21 citations in OpenAlex.
- Characterization of the thermophilic xylanase Fsa02490Xyn from the hyperthermophile Fervidibacter sacchari belonging to glycoside hydrolase family 10.FEBS open bio · 2025Article
- Cellulolytic and hemicellulolytic capacity of Acetivibrio clariflavus.Applied microbiology and biotechnology · 2025Review
- Whole-genome sequencing and genomic analysis of fourFrontiers in microbiology · 2024Article
- Recombinant production and characterization of full-length and truncated β-1,3-glucanase PglA from Paenibacillus sp. S09.BMC biotechnology · 2013Article
- Purification, characterization of GH11 endo-β-1,4-xylanase from thermotolerant Streptomyces sp. SWU10 and overexpression in Pichia pastoris KM71H.Molecular biotechnology · 2013Article
- Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.The Journal of biological chemistry · 2012Article
- A thermostable GH45 endoglucanase from yeast: impact of its atypical multimodularity on activity.Microbial cell factories · 2011Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A non-cellulosomal xylanase from Clostridium thermocellum, XynX, consists of a family-22 carbohydratebinding module (CBM22), a family-10 glycoside hydrolase (GH10) catalytic module, two family-9 carbohydrate-binding modules (CBM9-I and CBM9-II), and an S-layer homology (SLH) module. E. coli BL21(DE3) (pKM29), a transformant carrying xynX', produced several truncated forms of the enzyme. Among them, three major active species were purified by SDS-PAGE, activity staining, gel-slicing, and diffusion from the gel. The truncated xylanases were different from each other only in their C-terminal regions. In addition to the CBM22 and GH10 catalytic modules, XynX(1) had the CBM9-I and most of the CBM9-II, XynX(2) had the CBM9-I and about 40% of the CBM9-II, and XynX(3) had about 75% of the CBM9-I. The truncated xylanases showed higher binding capacities toward Avicel than those toward insoluble xylan. XynX(1) showed a higher affinity toward Avicel (70.5%) than XynX(2) (46.0%) and XynX(3) (42.1%); however, there were no significant differences in the affinities toward insoluble xylan. It is suggested that the CBM9 repeat, especially CBM9-II, of XynX plays a role in xylan degradation in nature by strengthening cellulose binding rather than by enhancing xylan binding.
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