ArticleBMC biochemistry2015
The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes.
Article in BMC biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 38 citations in OpenAlex.
- Surface Plasmon Resonance Analysis for Quantifying Protein-Carbohydrate Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cross-Feeding and Enzymatic Catabolism for Mannan-Oligosaccharide Utilization by the Butyrate-Producing Gut BacteriumMicroorganisms · 2022Article
- Impact of Modular Architecture on Activity of Glycoside Hydrolase Family 5 Subfamily 8 Mannanases.Molecules (Basel, Switzerland) · 2022Article
- Enzymatic Conversion of Mannan-Rich Plant Waste Biomass into Prebiotic Mannooligosaccharides.Foods (Basel, Switzerland) · 2021Review
- Structure and evolution of the bifidobacterial carbohydrate metabolism proteins and enzymes.Biochemical Society transactions · 2021Review
- Gene-Phenotype Associations Involving Human-Residential Bifidobacteria (HRB) Reveal Significant Species- and Strain-Specificity in Carbohydrate Catabolism.Microorganisms · 2021Article
- Carbohydrate-binding modules targeting branched polysaccharides: overcoming side-chain recalcitrance in a non-catalytic approach.Bioresources and bioprocessing · 2021Review
- Insights into the mechanism(s) of digestion of crystalline cellulose by plant class C GH9 endoglucanases.Journal of molecular modeling · 2019Article
- A surface-exposed GH26 β-mannanase fromThe Journal of biological chemistry · 2019Article
- β-Mannanase-catalyzed synthesis of alkyl mannooligosides.Applied microbiology and biotechnology · 2018Article
- Origin, evolution, and divergence of plant class C GH9 endoglucanases.BMC evolutionary biology · 2018Article
- Differential bacterial capture and transport preferences facilitate co-growth on dietary xylan in the human gut.Nature microbiology · 2018Article
- Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus: ENZYME SYNERGY AND CRYSTAL STRUCTURE OF A β-MANNANASE.The Journal of biological chemistry · 2017Article
- A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans.FEBS letters · 2016Article
- Proteinaceous Molecules Mediating Bifidobacterium-Host Interactions.Frontiers in microbiology · 2016Review
- Functional diversity of three tandem C-terminal carbohydrate-binding modules of a β-mannanase.The Journal of biological chemistryArticle
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundβ-Mannans are abundant and diverse plant structural and storage polysaccharides. Certain human gut microbiota members including health-promoting Bifidobacterium spp. catabolize dietary mannans. Little insight is available on the enzymology of mannan deconstruction in the gut ecological niche. Here, we report the biochemical properties of the first family 5 subfamily 8 glycoside hydrolase (GH5_8) mannanase from the probiotic bacterium Bifidobacterium animalis subsp. lactis Bl-04 (BlMan5_8).
resultsBlMan5_8 possesses a novel low affinity carbohydrate binding module (CBM) specific for soluble mannan and displays the highest catalytic efficiency reported to date for a GH5 mannanase owing to a very high k cat (1828 ± 87 s(-1)) and a low K m (1.58 ± 0.23 g · L(-1)) using locust bean galactomannan as substrate. The novel CBM of BlMan5_8 mediates increased binding to soluble mannan based on affinity electrophoresis. Surface plasmon resonance analysis confirmed the binding of the CBM10 to manno-oligosaccharides, albeit with slightly lower affinity than the catalytic module of the enzyme. This is the first example of a low-affinity mannan-specific CBM, which forms a subfamily of CBM10 together with close homologs present only in mannanases. Members of this new subfamily lack an aromatic residue mediating binding to insoluble cellulose in canonical CBM10 members consistent with the observed low mannan affinity.
conclusionBlMan5_8 is evolved for efficient deconstruction of soluble mannans, which is reflected by an exceptionally low K m and the presence of an atypical low affinity CBM, which increases binding to specifically to soluble mannan while causing minimal decrease in catalytic efficiency as opposed to enzymes with canonical mannan binding modules. These features highlight fine tuning of catalytic and binding properties to support specialization towards a preferred substrate, which is likely to confer an advantage in the adaptation to competitive ecological niches.
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