ArticleApplied and environmental microbiology2021
Alginate Degradation: Insights Obtained through Characterization of a Thermophilic Exolytic Alginate Lyase.
Article in Applied and environmental microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 40 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
- Alginate oligosaccharides in the food industry: emerging functional roles, health benefits, and technological applications - Review.Food chemistry: X · 2025Review
- Recent Advances in Alginate Lyase Engineering for Efficient Conversion of Alginate to Value-Added Products.Microbial biotechnology · 2025Review
- Diatom heterotrophy on brown algal polysaccharides emerged through horizontal gene transfer, gene duplication, and neofunctionalization.PLoS biology · 2025Article
- Identification and Characterization of a New Thermophilic κ-Carrageenan Sulfatase.Journal of agricultural and food chemistry · 2025Article
- 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
- Genome Sequencing-Based Mining and Characterization of a Novel Alginate Lyase fromMarine drugs · 2023Article
- Activation mechanism and activity of globupain, a thermostable C11 protease from the Arctic Mid-Ocean Ridge hydrothermal system.bioRxiv : the preprint server for biology · 2023Article
- Article
- Feasibility insights into the application ofFrontiers in microbiology · 2023Article
- Activation mechanism and activity of globupain, a thermostable C11 protease from the Arctic Mid-Ocean Ridge hydrothermal system.Frontiers in microbiology · 2023Article
- Enzymatic depolymerization of alginate by two novel thermostable alginate lyases fromFrontiers in plant science · 2022Article
- Structure-function analysis of a new PL17 oligoalginate lyase from the marine bacterium Zobellia galactanivorans DsijT.Glycobiology · 2021Article
- Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases.Marine drugs · 2021Review
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymatic depolymerization of seaweed polysaccharides is gaining interest for the production of functional oligosaccharides and fermentable sugars. Herein, we describe a thermostable alginate lyase that belongs to polysaccharide lyase family 17 (PL17) and was derived from an Arctic Mid-Ocean Ridge (AMOR) metagenomics data set. This enzyme, AMOR_PL17A, is a thermostable exolytic oligoalginate lyase (EC 4.2.2.26), which can degrade alginate, poly-β-d-mannuronate, and poly-α-l-guluronate within a broad range of pHs, temperatures, and salinity conditions. Site-directed mutagenesis showed that tyrosine Y251, previously suggested to act as a catalytic acid, indeed is essential for catalysis, whereas mutation of tyrosine Y446, previously proposed to act as a catalytic base, did not affect enzyme activity. The observed reaction products are protonated and deprotonated forms of the 4,5-unsaturated uronic acid monomer, Δ, two hydrates of DEH (4-deoxy-l-
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