ArticleMarine drugs2019
The Characterization and Modification of a Novel Bifunctional and Robust Alginate Lyase Derived from
Article in Marine drugs, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Inferring an ancestral alginate lyase for improved stability and high-level expression using fed-batch fermentation.Frontiers in microbiology · 2026Article
- Enhanced Thermostability and Catalytic Efficiency of Alginate Lyase Alyw203 by Hydrogen Bond Network Reconstruction.Marine drugs · 2025Article
- Heterologous Expression and Functional Characterization of a Truncated Marine Alginate Lyase.Applied biochemistry and biotechnology · 2025Article
- Genome Analysis of Alginate-Degrading BacteriumMicroorganisms · 2025Article
- Recent Advances in Alginate Lyase Engineering for Efficient Conversion of Alginate to Value-Added Products.Microbial biotechnology · 2025Review
- Multi-Functional Alginate LyaseMarine drugs · 2025Article
- Expression, Purification, and Characterisation of Recombinant Alginate Lyase (Molecules (Basel, Switzerland) · 2024Article
- Sustainable Production ofFoods (Basel, Switzerland) · 2024Review
- Characterization of bifunctional alginate lyase Aly644 and antimicrobial activity of enzymatic hydrolysates.Applied microbiology and biotechnology · 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
- Characterization of a Novel Polysaccharide Lyase Family 5 Alginate Lyase with PolyM Substrate Specificity.Foods (Basel, Switzerland) · 2022Article
- Cloning and Characterization of a Novel Endo-Type Metal-Independent Alginate Lyase from the Marine BacteriaMarine drugs · 2022Article
- Alginate Lyases from Marine Bacteria: An Enzyme Ocean for Sustainable Future.Molecules (Basel, Switzerland) · 2022Review
- Effects of Module Truncation of a New Alginate Lyase VxAly7C from MarineInternational journal of molecular sciences · 2022Article
- Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine BacteriumMarine drugs · 2022Article
- Evolving strategies for marine enzyme engineering: recent advances on the molecular modification of alginate lyase.Marine life science & technology · 2022Review
- Improving the thermostability of alginate lyase FlAlyA with high expression by computer-aided rational design for industrial preparation of alginate oligosaccharides.Frontiers in bioengineering and biotechnology · 2022Article
- Comparison of Biochemical Characteristics, Action Models, and Enzymatic Mechanisms of a Novel Exolytic and Two Endolytic Lyases with Mannuronate Preference.Marine drugs · 2021Article
- Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases.Marine drugs · 2021Review
- Purification and Characterization of a Novel Alginate Lyase from a MarineMarine drugs · 2021Article
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8 authors.
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Abstract
Alginase lyase is an important enzyme for the preparation of alginate oligosaccharides (AOS), that possess special biological activities and is widely used in various fields, such as medicine, food, and chemical industry. In this study, a novel bifunctional alginate lyase (AlgH) belonging to the PL7 family was screened and characterized. The AlgH exhibited the highest activity at 45 °C and pH 10.0, and was an alkaline enzyme that was stable at pH 6.0-10.0. The enzyme showed no significant dependence on metal ions, and exhibited unchanged activity at high concentration of NaCl. To determine the function of non-catalytic domains in the multi-domain enzyme, the recombinant AlgH-I containing only the catalysis domain and AlgH-II containing the catalysis domain and the carbohydrate binding module (CBM) domain were constructed and characterized. The results showed that the activity and thermostability of the reconstructed enzymes were significantly improved by deletion of the F5/8 type C domain. On the other hand, the substrate specificity and the mode of action of the reconstructed enzymes showed no change. Alginate could be completely degraded by the full-length and modified enzymes, and the main end-products were alginate disaccharide, trisaccharide, and tetrasaccharide. Due to the thermo and pH-stability, salt-tolerance, and bifunctionality, the modified alginate lyase was a robust enzyme which could be applied in industrial production of AOS.
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