In recent years, the research of fucoidans has steadily increased. The interest in these substances is due to their various biological activities. Despite a wide range of biological activity and the lack of oral toxicity, fucoidans remain relatively unexploited as a source of medicines because of their heterogeneity. Enzymes that degrade polyanionic polysaccharides are widely used for establishing their structures and structure-activity relationships. Sometimes, to obtain preparations of polysaccharides with standard characteristics, for example, medicines and food supplements, enzymatic treatment can be also applied. Only a few sources of enzymes with fucoidanase activity have been described, and only a few studies regarding the isolation and characterization of fucoidanases have been performed. The data on the specificity of fucoidanases: the type of cleaved glycoside bond, the relation between catalytic activity and the degree of substrate sulfation are scarce. The review summarizes achievements in the research of fucoidanases, mechanisms of enzymatic degradation of fucoidans, as well as of structures of sulfated fucooligosaccharides obtained under the action of fucoidanases.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1093/glycob/cwv072 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Targeted metagenomics - Enrichment for enzymes active on sulfated polysaccharides from seaweeds.
Enzyme Microb Technol
January 2025
Matis ohf, Vínlandsleið 12, Reykjavík 113, Iceland; University of Iceland, Sæmundargata 2, Reykjavík 102, Iceland.
Seaweeds (macroalgae) are an attractive resource for diverse microbial- and enzymatic production processes. They are abundant, underutilized, cheap, and rich in carbohydrates, and therefore have the potential to be used as a source of mono- or oligosaccharides, and as substrates for industrial fermentation processes. Many seaweed polysaccharides, including the sulfated polysaccharides ulvan and fucoidan, are however complex and heterogenous in structure, and there are currently few enzymes available to modify them, and understanding of their enzymatic depolymerization remains limited.
View Article and Find Full Text PDFApplication of MALDI-MS for characterization of fucoidan hydrolysates and screening of endo-fucoidanase activity.
Carbohydr Polym
September 2024
Department of Chemistry, Biotechnology, and Life Science, Norwegian University of Life Sciences (NMBU), Christian Magnus Falsens vei 18, 1433 Ås, Norway. Electronic address:
Article Synopsis
- - Brown macroalgae produce fucoidans, which are sulfated polysaccharides that help with carbon dioxide sequestration and have potential uses in biotech and medicine, but their structural diversity complicates their application.
- - The study uses MALDI mass spectrometry alongside biocatalysis to demonstrate that enzymes can create defined oligosaccharide structures from raw macroalgal biomass, showcasing a versatile approach applicable across multiple algae species.
- - The research establishes that this method, utilizing both MALDI-TOF/TOF and AP-MALDI-Orbitrap technologies, allows for efficient extraction and high-throughput evaluation of fucoidan samples, facilitating better understanding and utilization of these compounds.
The Discovery of the Fucoidan-Active Endo-1→4-α-L-Fucanase of the GH168 Family, Which Produces Fucoidan Derivatives with Regular Sulfation and Anticoagulant Activity.
Int J Mol Sci
December 2023
Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 159, Prospect 100-Let Vladivostoku, 690022 Vladivostok, Russia.
Sulfated polysaccharides of brown algae, fucoidans, are known for their anticoagulant properties, similar to animal heparin. Their complex and irregular structure is the main bottleneck in standardization and in defining the relationship between their structure and bioactivity. Fucoidan-active enzymes can be effective tools to overcome these problems.
View Article and Find Full Text PDFStructural and functional characterization of the novel endo-α(1,4)-fucoidanase Mef1 from the marine bacterium Muricauda eckloniae.
Acta Crystallogr D Struct Biol
November 2023
Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, DK-2800 Kgs Lyngby, Denmark.
Fucoidanases (EC 3.2.1.
View Article and Find Full Text PDFPurification and Characterization of the Enzyme Fucoidanase from Utilizing Fucoidan from .
Foods
April 2023
Key Laboratory of Aquatic Products Processing and Utilization of Liaoning Province, National R and D Branch Center for Seaweed Processing, College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, China.
Fucoidanase is an unstable enzyme with high specificity that requires a large about of time to screen it from microorganisms. In this study, enzymatic hydrolysis was used to produce low-molecular-weight fucoidan from microorganisms via the degradation of high-molecular-weight fucoidan without damage to the sulfate esterification structure of oligosaccharide. The microbial strain HN-25 was isolated from sea mud and was made to undergo mutagenicity under ultraviolet light.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!