ArticlePloS one2014
Characterization of AlgMsp, an alginate lyase from Microbulbifer sp. 6532A.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 82 citations in OpenAlex.
- Dissecting a two-domain alginate lyase of family PL6 reveals a mechanistic basis for substrate specificity and enzyme activity.The Journal of biological chemistry · 2026Article
- A comparative study of the efficacy of alginate lyases in the presence of metal ions elevated in the cystic fibrosis lung milieu.Biochemistry and biophysics reports · 2024Article
- Expression, Purification, and Characterisation of Recombinant Alginate Lyase (Molecules (Basel, Switzerland) · 2024Article
- Genome Analysis of Multiple Polysaccharide-Degrading Bacterium Microbulbifer thermotolerans HB226069: Determination of Alginate Lyase Activity.Marine biotechnology (New York, N.Y.) · 2024Article
- Polymer degrading marineBeilstein journal of organic chemistry · 2024Review
- A Recombinant Alginate Lyase Algt1 with Potential in Preparing Alginate Oligosaccharides at High-Concentration Substrate.Foods (Basel, Switzerland) · 2023Article
- Three alginate lyases provide a new gutApplied and environmental microbiology · 2023Article
- Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily.Frontiers in microbiology · 2023Article
- Synergy of the Two Alginate Lyase Domains of a Novel Alginate Lyase fromApplied and environmental microbiology · 2022Article
- Insights into the Influence of Signal Peptide on the Enzymatic Properties of Alginate Lyase AlyI1 with Removal Effect onMarine drugs · 2022Article
- Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine BacteriumMarine drugs · 2022Article
- Alginate Lyases from Marine Bacteria: An Enzyme Ocean for Sustainable Future.Molecules (Basel, Switzerland) · 2022Review
- Characterization of a New Biofunctional, Exolytic Alginate Lyase fromMarine drugs · 2021Article
- Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine BacteriumMarine drugs · 2021Article
- Specificities and Synergistic Actions of Novel PL8 and PL7 Alginate Lyases from the Marine FungusJournal of fungi (Basel, Switzerland) · 2021Article
- Secretory Expression of an Alkaline Alginate Lyase With Heat Recovery Property inFrontiers in microbiology · 2021Article
- Recent progress on engineering microbial alginate lyases towards their versatile role in biotechnological applications.Folia microbiologica · 2020Review
- Biochemical and computational study of an alginate lyase produced byIranian journal of basic medical sciences · 2020Article
- Purification and Characterization of a Novel Endolytic Alginate Lyase fromMarine drugs · 2020Article
- Characterization and Application of an Alginate Lyase, Aly1281 from Marine BacteriumMarine drugs · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alginate is a polysaccharide produced by certain seaweeds and bacteria that consists of mannuronic acid and guluronic acid residues. Seaweed alginate is used in food and industrial chemical processes, while the biosynthesis of bacterial alginate is associated with pathogenic Pseudomonas aeruginosa. Alginate lyases cleave this polysaccharide into short oligo-uronates and thus have the potential to be utilized for both industrial and medicinal applications. An alginate lyase gene, algMsp, from Microbulbifer sp. 6532A, was synthesized as an E.coli codon-optimized clone. The resulting 37 kDa recombinant protein, AlgMsp, was expressed, purified and characterized. The alginate lyase displayed highest activity at pH 8 and 0.2 M NaCl. Activity of the alginate lyase was greatest at 50°C; however the enzyme was not stable over time when incubated at 50°C. The alginate lyase was still highly active at 25°C and displayed little or no loss of activity after 24 hours at 25°C. The activity of AlgMsp was not dependent on the presence of divalent cations. Comparing activity of the lyase against polymannuronic acid and polyguluronic acid substrates showed a higher turnover rate for polymannuronic acid. However, AlgMSP exhibited greater catalytic efficiency with the polyguluronic acid substrate. Prolonged AlgMsp-mediated degradation of alginate produced dimer, trimer, tetramer, and pentamer oligo-uronates.
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