ArticleApplied and environmental microbiology2014
Bifidobacterium longum subsp. longum Exo-β-1,3-Galactanase, an enzyme for the degradation of type II arabinogalactan.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Crystal structure of endo-β-1,6-galactanase from Streptomyces avermitilis.Acta crystallographica. Section D, Structural biology · 2026Article
- β-galactanase: an effective tool for the degradation of plant β-ᴅ-galactan.World journal of microbiology & biotechnology · 2025Review
- Structure and function of a β-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium.Communications biology · 2025Article
- Bifidobacterial GH146 β-L-arabinofuranosidase for the removal of β1,3-L-arabinofuranosides on plant glycans.Applied microbiology and biotechnology · 2024Article
- Collateral beauty in the damages: an overview of cosmetics and therapeutic applications of microbial proteases.Archives of microbiology · 2023Review
- Assimilation of arabinogalactan side chains with novel 3-Microbiome research reports · 2023Article
- Molecular Cloning and Characterization of a Novel Exo-β-1,3-Galactanase fromJournal of microbiology and biotechnology · 2022Article
- Microbial liberation of N-methylserotonin from orange fiber in gnotobiotic mice and humans.Cell · 2022Article
- Mechanism of Cooperative Degradation of Gum Arabic Arabinogalactan Protein by Bifidobacterium longum Surface Enzymes.Applied and environmental microbiology · 2022Article
- Two α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum are involved in arabinoxylan utilization.Applied microbiology and biotechnology · 2022Article
- Chemical and nutritional characteristics, and microbial degradation of rapeseed meal recalcitrant carbohydrates: A review.Frontiers in nutrition · 2022Review
- Captive Common Marmosets (Callithrix jacchus) Are Colonized throughout Their Lives by a Community ofmBio · 2021Article
- Novel 3-Applied and environmental microbiology · 2021Article
- The Role of Arabinogalactan Type II Degradation in Plant-Microbe Interactions.Frontiers in microbiology · 2021Review
- Plant Glycan Metabolism by Bifidobacteria.Frontiers in microbiology · 2021Review
- Biochemical analysis of cross-feeding behaviour between two common gut commensals when cultivated on plant-derived arabinogalactan.Microbial biotechnology · 2020Article
- Arabinogalactan Utilization byMicroorganisms · 2020Article
- Article
- Two Novel α-l-Arabinofuranosidases fromApplied and environmental microbiology · 2019Article
- Genomic diversity and distribution of Bifidobacterium longum subsp. longum across the human lifespan.Scientific reports · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type II arabinogalactan (AG-II) is a suitable carbohydrate source for Bifidobacterium longum subsp. longum, but the degradative enzymes have never been characterized. In this study, we characterized an exo-β-1,3-galactanase, BLLJ_1840, belonging to glycoside hydrolase family 43 from B. longum subsp. longum JCM1217. The recombinant BLLJ_1840 expressed in Escherichia coli hydrolyzed β-1,3-linked galactooligosaccharides but not β-1,4- and β-1,6-linked galactooligosaccharides. The enzyme also hydrolyzed larch wood arabinogalactan (LWAG), which comprises a β-1,3-linked galactan backbone with β-1,6-linked galactan side chains. The kcat/Km ratio of dearabinosylated LWAG was 24-fold higher than that of β-1,3-galactan. BLLJ_1840 is a novel type of exo-β-1,3-galactanase with a higher affinity for the β-1,6-substituted β-1,3-galactan than for nonsubstituted β-1,3-galactan. BLLJ_1840 has 27% to 28% identities with other characterized exo--1,3-galactanases from bacteria and fungi. The homologous genes are conserved in several strains of B. longum subsp. longum and B. longum subsp. infantis but not in other bifidobacteria. Transcriptional analysis revealed that BLLJ_1840 is intensively induced with BLLJ_1841, an endo-β-1,6-galactanase candidate, in the presence of LWAG. This is the first report of exo-β-1,3-galactanase in bifidobacteria, which is an enzyme used for the acquisition of AG-II in B. longum subsp. longum.
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