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.

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.

Sulfated polysaccharides accelerate gliadin digestion and reduce its toxicity.

Celiac disease and other types of gluten intolerance significantly affect the life quality of patients making them restrict the diet removing all food produced from wheat, rye, oat, and barley flour, and some other products. These disorders arise from protease resistance of poorly soluble proteins prolamins, contained in gluten. Enhanced proteolytic digestion of gliadins might be considered as a prospective approach for the treatment of celiac disease and other types of gluten intolerance.

Control of postprandial hyperglycemia by oral administration of the sea anemone mucus-derived α-amylase inhibitor (magnificamide).

Diabetes mellitus is a serious threat to human health in both developed and developing countries. Optimal disease control requires the use of a diet and a combination of several medications, including oral hypoglycemic agents such as α-glucosidase inhibitors. Currently, the arsenal of available drugs is insufficient, which determines the relevance of studying new potent α-amylase inhibitors.

Structure and Metabolically Oriented Efficacy of Fucoidan from Brown Alga in the Model of Colony Formation of Melanoma and Breast Cancer Cells.

This work reports the detailed structure of fucoidan from (2SmF2) and its ability to potentiate the inhibitory effect of glycolysis inhibitor 2-deoxy-d-glucose (2-DG). 2SmF2 was shown to be sulfated and acetylated galactofucan containing a main chain of alternating residues of 1,3- and 1,4-linked α-l-fucopyranose, fucose fragments with monotonous 1,3- and 1,4-type linkages (DP up to 3), α-d-Gal-(1→3)-α-L-Fuc disaccharides, and 1,3,4- and 1,2,4-linked fucose branching points. The sulfate groups were found at positions 2 and 4 of fucose and galactose residues.

Production of high- and low-molecular weight fucoidan fragments with defined sulfation patterns and heightened in vitro anticancer activity against TNBC cells using novel endo-fucanases of the GH107 family.

Fucoidans are complex fucose-containing sulfated polysaccharides with pronounced anticancer effects. Their structure-anticancer activity relationships are difficult to determine due to fucoidans' complex, often irregularities-including structures. Fucoidan-active enzymes can be used for this propose.

Pectins from the sea grass Enhalus acoroides (L.f.) Royle: Structure, biological activity and ability to form nanoparticles.

Two pectins from the seagrass Enhalus acoroides (L.f.) Royle were isolated for the first time.

Fucoidan-active α-L-fucosidases of the GH29 and GH95 families from a fucoidan degrading cluster of the marine bacterium Wenyingzhuangia fucanilytica.

In present work we provide the bioinformatic and biochemical characterization of six α-L-fucosidases that belong to the 29 and 95 families of glycoside hydrolases (GH) from the fucoidan-degrading locus of the marine bacterium Wenyingzhuangia fucanilytica CZ1127. The fucosidases FucWf1, FucWf2, FucWf3 and FucWf6 are relegated to the subfamily A of the GH29 family. The fucosidase FucWf4 bears a distant resemblance to the GH29 and does not belong to either the GH29A or the GH29B subfamilies.

Two GH16 Endo-1,3-β-D-Glucanases from Formosa agariphila and F. algae Bacteria Have Complete Different Modes of Laminarin Digestion.

There is a comparative analysis of primary structures and catalytic properties of two recombinant endo-1,3-β-D-glucanases from marine bacteria Formosa agariphila KMM 3901 and previously reported F. algae KMM 3553. Both enzymes had the same molecular mass 61 kDa, temperature optimum 45 °C, and comparable ranges of thermal stability and Km.

Discovery of a fucoidan endo-4O-sulfatase: Regioselective 4O-desulfation of fucoidans and its effect on anticancer activity in vitro.

Fucoidans are a class of sulfated fucose-containing bioactive polysaccharides produced by brown algae. The biological effects exhibited by fucoidans are thought to be related to their sulfation. However, the lack of methods for sulfation control does not allow for a reliable conclusion about the influence of the position of certain sulfate groups on the observed biological effects.

Relationship between the structure of a highly regular fucoidan from Fucus evanescens and its ability to form nanoparticles.

Chitosan/fucoidan nanoparticles were created using two fucoidans from the Fucus evanescens algae. One of them was a regular fucoidan obtained for the first time from the alga harvested at the reproductive growth stage, using only standard extraction methods, without additional modifications. Its structure was established via NMR spectroscopy to consist of the repeating →3)-α-L-Fucp-(2,4SO)-(1 → 4)-α-L-Fucp-(2SO)-(1→ fragment.

Expression and biochemical characterization of two recombinant fucoidanases from the marine bacterium Wenyingzhuangia fucanilytica CZ1127.

Genomic analysis of the marine bacterium Wenyingzhuangia fucanilytica CZ1127 revealed the presence of four fucoidanase genes fwf1, fwf2, fwf3, fwf4 that belonged to the glycoside hydrolase family 107 (GH107, CAZy), which is located in one gene cluster putatively involved in fucoidan catabolism. Genes encoding two fucoidanases fwf1 and fwf2 were cloned, and the proteins FWf1 and FWf2 were produced in Escherichia coli cells. The recombinant fucoidanases were purified and the biochemical properties of these enzymes were studied.

Enzymatic transformation and anti-tumor activity of Sargassum horneri fucoidan.

Structure of the fucoidan from Sargassum horneri and products of its enzymatic transformation with molecular weight over 20 kDa were investigated. Fucoidan was hydrolyzed by recombinant fucoidanase FFA1 and its fraction of higher molecular weight was fractionated using anion-exchange chromatography, resulting in three sulphated polysaccharides of various molecular weight (63-138 kDa). Their structures were analyzed using NMR spectroscopy, showing the fucoidan (ShF) to be a branched polysaccharide with the backbone consisting of the repeating →3-α-l-Fucp(2SO)-1→4-α-l-Fucp(2,3SO)-1→ fragment and side chains including the α-l-Fucp-1→2-α-l-Fucp-1→ or α-l-Fucp-1→3-α-l-Fucp(4SO)-1→ fragments attached to the main chain at C4.

Laminarans and 1,3-β-D-glucanases.

The laminarans are biologically active water-soluble polysaccharide (1,3;1,6-β-D-glucans) of brown algae. These polysaccharides are an attractive object for research due to its relatively simple structure, low toxicity, and various biological effects. 1,3-β-D-glucanases are an effective tool for studying the structure of laminarans, and can also be used to obtain new biologically active derivatives.

Two New Alginate Lyases of PL7 and PL6 Families from Polysaccharide-Degrading Bacterium KMM 3553: Structure, Properties, and Products Analysis.

A bifunctional alginate lyase (ALFA3) and mannuronate-specific alginate lyase (ALFA4) genes were found in the genome of polysaccharide-degrading marine bacterium KMM 3553. They were classified to PL7 and PL6 polysaccharide lyases families and expressed in . The recombinant ALFA3 appeared to be active both on mannuronate- and guluronate-enriched alginates, as well as pure sodium mannuronate.

Radiosensitizing effect of the fucoidan from brown alga Fucus evanescens and its derivative in human cancer cells.

Fucoidan from brown alga Fucus evanescens and its product of enzymatic hydrolysis have precisely established structure and possess significant biological activities. The aim of present study was to determine radiosensitizing activity of fucoidan from brown alga F. evanescens and its derivative in human melanoma, breast adenocarcinoma, and colorectal carcinoma cell lines and elucidate mechanism of their action.

Novel Enzyme Actions for Sulphated Galactofucan Depolymerisation and a New Engineering Strategy for Molecular Stabilisation of Fucoidan Degrading Enzymes.

Fucoidans from brown macroalgae have beneficial biomedical properties but their use as pharma products requires homogenous oligomeric products. In this study, the action of five recombinant microbial fucoidan degrading enzymes were evaluated on fucoidans from brown macroalgae: , , , , , and . The enzymes included three endo-fucoidanases (EC 3.

Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127.

Fucoidans belong to a structurally heterogeneous class of sulfated polysaccharides isolated from brown algae. They have a wide spectrum of biological activities. The complex structures of these polysaccharides hinder structure-activity relationships determination.

Modification of native fucoidan from Fucus evanescens by recombinant fucoidanase from marine bacteria Formosa algae.

Enzymatic depolymerization of fucoidans attracts many researchers due to the opportunity of obtaining standardized fucoidan fragments. Fucoidanase catalyzes the cleavage of fucoidan from Fucus evanescens (FeF) to form low molecular weight products (LMP) and a polymeric fraction (HMP) with 50.8 kDa molecular weight and more than 50% yield.

Structure, enzymatic transformation, anticancer activity of fucoidan and sulphated fucooligosaccharides from Sargassum horneri.

Structure and anticancer activity of fucoidan from Sargassum horneri and from products of its enzymatic transformation were investigated. A gene that encodes fucoidanase ffa1 in the marine bacteria F. algae was identified, cloned and the protein (FFA1) was produced in Escherichia coli.

A new recombinant endo-1,3-β-D-glucanase from the marine bacterium Formosa algae KMM 3553: enzyme characteristics and transglycosylation products analysis.

A specific endo-1,3-β-D-glucanase (GFA) gene was found in genome of marine bacterium Formosa algae KMM 3553. For today this is the only characterized endo-1,3-β-D-glucanase (EC 3.2.

Expression and biochemical characterization and substrate specificity of the fucoidanase from Formosa algae.

A gene that encodes fucoidanase ffa2 in the marine bacterium Formosa algae strain KMM 3553T was cloned, and the protein (FFA2) was produced in Escherichia coli. Recombinant fucoidanase FFA2 was purified, and the biochemical properties of this enzyme were studied. The amino acid sequence of FFA2 showed 57% identity with known fucoidanase FcnA from Mariniflexile fucanivorans.

Structure and biological activity of a fucosylated chondroitin sulfate from the sea cucumber Cucumaria japonica.

A fucosylated chondroitin sulfate (FCS) was isolated from the body wall of Pacific sea cucumber Cucumaria japonicaby extraction in the presence of papain followed by Cetavlon precipitation and anion-exchange chromatography. FCS was shown to contain D-GalNAc, D-GlcA, L-Fuc and sulfate in molar proportions of about 1:1:1:4.5.

Fucoidanases.

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.