ArticleScientific reports2020
Functional characterization of three Azotobacter chroococcum alginate-modifying enzymes related to the Azotobacter vinelandii AlgE mannuronan C-5-epimerase family.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 33 citations in OpenAlex.
- Mode of Action of AlgE1: A Modular Mannuronate C-5 Epimerase.Biochemistry · 2025Article
- Immobilization of alginate C-5 epimerases usingApplied and environmental microbiology · 2025Article
- Advances in alginate biosynthesis: regulation and production inFrontiers in bioengineering and biotechnology · 2025Review
- Candidate genes involved in biosynthesis and degradation of the main extracellular matrix polysaccharides of brown algae and their probable evolutionary history.BMC genomics · 2024Article
- Identification and statistical optimization of a novel alginate polymer extracted from newly isolated Synechocystis algini MNE ON864447 with antibacterial activity.Microbial cell factories · 2023Article
- Molecular insights into alginate β-lactoglobulin A multivalencies-The foundation for their amorphous aggregates and coacervation.Protein science : a publication of the Protein Society · 2023Article
- Computational modeling of the molecular basis for the calcium-dependence of the mannuronan C-5 epimerase AvAlgE6 fromComputational and structural biotechnology journal · 2023Article
- Mechanistic Basis for Understanding the Dual Activities of the Bifunctional Azotobacter vinelandii Mannuronan C-5-Epimerase and Alginate Lyase AlgE7.Applied and environmental microbiology · 2022Article
- Strain Construction and Process Development for Efficient Recombinant Production of Mannuronan C-5 Epimerases inFrontiers in plant science · 2022Article
- Seaweed-Derived Alginate-Cellulose Nanofiber Aerogel for Insulation Applications.ACS applied materials & interfaces · 2021Article
- Rhamnolipid Enhances the Nitrogen Fixation Activity ofFrontiers in microbiology · 2021Article
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6 authors at 1 institution in 1 country.
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Abstract
Bacterial alginate initially consists of 1-4-linked β-D-mannuronic acid residues (M) which can be later epimerized to α-L-guluronic acid (G). The family of AlgE mannuronan C-5-epimerases from Azotobacter vinelandii has been extensively studied, and three genes putatively encoding AlgE-type epimerases have recently been identified in the genome of Azotobacter chroococcum. The three A. chroococcum genes, here designated AcalgE1, AcalgE2 and AcalgE3, were recombinantly expressed in Escherichia coli and the gene products were partially purified. The catalytic activities of the enzymes were stimulated by the addition of calcium ions in vitro. AcAlgE1 displayed epimerase activity and was able to introduce long G-blocks in the alginate substrate, preferentially by attacking M residues next to pre-existing G residues. AcAlgE2 and AcAlgE3 were found to display lyase activities with a substrate preference toward M-alginate. AcAlgE2 solely accepted M residues in the positions - 1 and + 2 relative to the cleavage site, while AcAlgE3 could accept either M or G residues in these two positions. Both AcAlgE2 and AcAlgE3 were bifunctional and could also catalyze epimerization of M to G. Together, we demonstrate that A. chroococcum encodes three different AlgE-like alginate-modifying enzymes and the biotechnological and biological impact of these findings are discussed.
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