ArticleApplied and environmental microbiology2014
Comparative biochemical characterization of three exolytic oligoalginate lyases from Vibrio splendidus reveals complementary substrate scope, temperature, and pH adaptations.
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 51 papers.
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51 citing papers in PubMed, 109 citations in OpenAlex.
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- Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1.Microorganisms · 2024Article
- Exploring potential polysaccharide utilization loci involved in the degradation of typical marine seaweed polysaccharides byFrontiers in microbiology · 2024Article
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- A Novel Cold-Adapted and High-Alkaline Alginate Lyase with Potential for Alginate Oligosaccharides Preparation.Molecules (Basel, Switzerland) · 2023Article
- Utilization of Macroalgae for the Production of Bioactive Compounds and Bioprocesses Using Microbial Biotechnology.Microorganisms · 2023Review
- A novel alginate lyase and its domain functions for the preparation of unsaturated monosaccharides.Applied microbiology and biotechnology · 2023Article
- Characterization of Multiple Alginate Lyases in a Highly Efficient Alginate-DegradingApplied and environmental microbiology · 2022Article
- Synergy of the Two Alginate Lyase Domains of a Novel Alginate Lyase fromApplied and environmental microbiology · 2022Article
- A Novel Carrageenan Metabolic Pathway in Flavobacterium algicola.Applied and environmental microbiology · 2022Article
- Determination of oligosaccharide product distributions of PL7 alginate lyases by their structural elements.Communications biology · 2022Article
- Bacterial growth in multicellular aggregates leads to the emergence of complex life cycles.Current biology : CB · 2022Article
- Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine BacteriumMarine drugs · 2022Article
- Sustainable alginate lyases catalyzed degradation of bio-based carbohydrates.Frontiers in chemistry · 2022Review
- Microbial Regulation of Deterioration and Preservation of Salted Kelp under Different Temperature and Salinity Conditions.Foods (Basel, Switzerland) · 2021Article
- Bacterial alginate metabolism: an important pathway for bioconversion of brown algae.Biotechnology for biofuels · 2021Review
- Alginate Degradation: Insights Obtained through Characterization of a Thermophilic Exolytic Alginate Lyase.Applied and environmental microbiology · 2021Article
- Secretory Expression of an Alkaline Alginate Lyase With Heat Recovery Property inFrontiers in microbiology · 2021Article
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5 authors at 3 institutions in 2 countries.
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Abstract
Marine microbes use alginate lyases to degrade and catabolize alginate, a major cell wall matrix polysaccharide of brown seaweeds. Microbes frequently contain multiple, apparently redundant alginate lyases, raising the question of whether these enzymes have complementary functions. We report here on the molecular cloning and functional characterization of three exo-type oligoalginate lyases (OalA, OalB, and OalC) from Vibrio splendidus 12B01 (12B01), a marine bacterioplankton species. OalA was most active at 16°C, had a pH optimum of 6.5, and displayed activities toward poly-β-d-mannuronate [poly(M)] and poly-α-l-guluronate [poly(G)], indicating that it is a bifunctional enzyme. OalB and OalC were most active at 30 and 35°C, had pH optima of 7.0 and 7.5, and degraded poly(M·G) and poly(M), respectively. Detailed kinetic analyses of oligoalginate lyases with poly(G), poly(M), and poly(M·G) and sodium alginate as substrates demonstrated that OalA and OalC preferred poly(M), whereas OalB preferred poly(M·G). The catalytic efficiency (kcat/Km) of OalA against poly(M) increased with decreasing size of the substrate. OalA showed kcat/Km from 2,130 mg(-1) ml s(-1) for the trisaccharide to 224 mg(-1) ml s(-1) for larger oligomers of ∼50 residues, and 50.5 mg(-1) ml s(-1) for high-molecular-weight alginate. Although OalA was most active on the trisaccharide, OalB and OalC preferred dimers. Taken together, our results indicate that these three Oals have complementary substrate scopes and temperature and pH adaptations.
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