ArticleApplied and environmental microbiology2006
Characterization of an exo-beta-1,3-galactanase from Clostridium thermocellum.
Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 52 citations in OpenAlex.
- Crystal structure of endo-β-1,6-galactanase from Streptomyces avermitilis.Acta crystallographica. Section D, Structural biology · 2026Article
- Functional and structural characterization of AtAbf43C: an exo-1,5-α-L-arabinofuranosidase from Acetivibrio thermocellus DSM1313.The Biochemical journal · 2025Article
- Cellulolytic and hemicellulolytic capacity of Acetivibrio clariflavus.Applied microbiology and biotechnology · 2025Review
- Structure and function of a β-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium.Communications biology · 2025Article
- The Crystal Structure ofToxins · 2022Article
- Molecular Cloning and Characterization of a Novel Exo-β-1,3-Galactanase fromJournal of microbiology and biotechnology · 2022Article
- Chemical and nutritional characteristics, and microbial degradation of rapeseed meal recalcitrant carbohydrates: A review.Frontiers in nutrition · 2022Review
- Novel 3-Applied and environmental microbiology · 2021Article
- Plant Glycan Metabolism by Bifidobacteria.Frontiers in microbiology · 2021Review
- The Role of Arabinogalactan Type II Degradation in Plant-Microbe Interactions.Frontiers in microbiology · 2021Review
- Unique active-site and subsite features in the arabinogalactan-degrading GH43 exo-β-1,3-galactanase fromThe Journal of biological chemistry · 2020Article
- Golgi-localized exo-β1,3-galactosidases involved in cell expansion and root growth inThe Journal of biological chemistry · 2020Article
- A surface endogalactanase in Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation.Nature microbiology · 2018Article
- Optimizing the composition of a synthetic cellulosome complex for the hydrolysis of softwood pulp: identification of the enzymatic core functions and biochemical complex characterization.Biotechnology for biofuels · 2018Article
- Enzymatic and Chemoenzymatic Syntheses of Disialyl Glycans and Their Necrotizing Enterocolitis Preventing Effects.The Journal of organic chemistry · 2017Article
- Enzymatic diversity of the Clostridium thermocellum cellulosome is crucial for the degradation of crystalline cellulose and plant biomass.Scientific reports · 2016Article
- Bifidobacterium longum subsp. longum Exo-β-1,3-Galactanase, an enzyme for the degradation of type II arabinogalactan.Applied and environmental microbiology · 2014Article
- Arabinogalactan proteins: focus on carbohydrate active enzymes.Frontiers in plant science · 2014Review
- Structural characterization of Arabidopsis leaf arabinogalactan polysaccharides.Plant physiology · 2012Article
- An exo-β-(1→3)-D-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure.Carbohydrate research · 2012Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A gene encoding an exo-beta-1,3-galactanase from Clostridium thermocellum, Ct1,3Gal43A, was isolated. The sequence has similarity with an exo-beta-1,3-galactanase of Phanerochaete chrysosporium (Pc1,3Gal43A). The gene encodes a modular protein consisting of an N-terminal glycoside hydrolase family 43 (GH43) module, a family 13 carbohydrate-binding module (CBM13), and a C-terminal dockerin domain. The gene corresponding to the GH43 module was expressed in Escherichia coli, and the gene product was characterized. The recombinant enzyme shows optimal activity at pH 6.0 and 50 degrees C and catalyzes hydrolysis only of beta-1,3-linked galactosyl oligosaccharides and polysaccharides. High-performance liquid chromatography analysis of the hydrolysis products demonstrated that the enzyme produces galactose from beta-1,3-galactan in an exo-acting manner. When the enzyme acted on arabinogalactan proteins (AGPs), the enzyme produced oligosaccharides together with galactose, suggesting that the enzyme is able to accommodate a beta-1,6-linked galactosyl side chain. The substrate specificity of the enzyme is very similar to that of Pc1,3Gal43A, suggesting that the enzyme is an exo-beta-1,3-galactanase. Affinity gel electrophoresis of the C-terminal CBM13 did not show any affinity for polysaccharides, including beta-1,3-galactan. However, frontal affinity chromatography for the CBM13 indicated that the CBM13 specifically interacts with oligosaccharides containing a beta-1,3-galactobiose, beta-1,4-galactosyl glucose, or beta-1,4-galactosyl N-acetylglucosaminide moiety at the nonreducing end. Interestingly, CBM13 in the C terminus of Ct1,3Gal43A appeared to interfere with the enzyme activity toward beta-1,3-galactan and alpha-l-arabinofuranosidase-treated AGP.
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