Glycosidases of marine organisms.

This review discusses the catalytic properties, activity regulation, structure, and functions of O-glycoside hydrolases from marine organisms exemplified by endo-1→3-β-D-glucanases of marine invertebrates.

[Extracellular beta-D-glucosidase of the Penicillium canescens marine fungus].

Extracellular beta-D-glucosidase was isolated in a homogeneous state from the Penicillium canescens marine fungus. According to SDS-electrophoresis, the molecular weight of the enzyme was 64 kDa and the maximal activity was observed at pH 5.2 and 70 degrees C.

Catalytic properties and amino acid sequence of endo-1→3-β-D-glucanase from the marine mollusk Tapes literata.

A specific 1→3-β-D-glucanase with molecular mass 37 kDa was isolated in homogeneous state from crystalline style of the commercial marine mollusk Tapes literata. It exhibits maximal activity within the pH range from 4.5 to 7.

[Distribution of O-glycosylases in marine fungi of the Sea of Japan and the Sea of Okhotsk: characterization of exocellular N-acetyl-beta-D-glucosaminidase of the marine fungus Penicillium canescens].

The capacity to produce exocellular enmzymes was studied for 92 samples of fungi from various marine habitats in the Sea of Okhotsk (78 strains) and the Sea of Japan (14 strains). Strains producing highly active glycanases and glycosidases were found. Synthesis of O-glycosylhydrolases was stimulated by addition of laminaran to the nutrient medium.

Enzymatic and molecular characterization of an endo-1,3-β-d-glucanase from the crystalline styles of the mussel Perna viridis.

The retaining endo-1,3-β-d-glucanase (EC 3.2.1.

[Catalytic properties of endo-1,3-beta-D-glucanase from the Vietnamese edible mussel Perna viridis].

A beta-1,3-glucanase with a molecular mass of 33 kDa was isolated in the homogeneous state from a crystalline stalk of the commercially available Vietnamese edible mussel Perna viridis. It hydrolyzes beta-1,3-bonds in glucans and is capable of catalyzing the transglycosylation reaction. The beta-1,3-glucanase has a K(m) value of 0.

[O-glycosylhydrolases of embryos of the sea urchin Strongylocentrotus intermedius and effect of some natural substances on their biosynthesis].

Embryos of sea urchin Strongylocentrotus intermedius have been revealed to contain o-glycosylhydrolases: highly active 1,3-beta-D-glucanase and alpha-D-mannosidase as well as a lower activity of beta-D-glucosidase and beta-D-galactosidase. Dynamics of changes of the enzyme activities has been studied at various stages of the sea urchin embryo development. There also have been studied effects of some substances (natural fucoidans, beta-1,3; 1,6-glucans formed by enzymatic synthesis as well as a protein inhibitor of marine mollusc endo-1,3-beta-D-glucanases) on development of the embryos and biosynthesis of 1,3-beta-D-glucanase and alpha-D-mannosidase.

Catalytic properties and mode of action of endo-(1-->3)-beta-D-glucanase and beta-D-glucosidase from the marine mollusk Littorina kurila.

A complex of the enzymes from the liver of the marine mollusk Littorina kurila that hydrolyzes laminaran was investigated. Two (1-->3)-beta-d-glucanases (G-I and G-II) were isolated. The molecular mass of G-I as estimated by gel-permeation chromatography and SDS-PAGE analysis was 32 and 40kDa, respectively.

Structure, biological activity, and enzymatic transformation of fucoidans from the brown seaweeds.

Recent advances in the study of fucoidans, biologically active sulfated alpha-L-fucans of diverse structures and synthesized exclusively by marine organisms, are overviewed. Their structure, biological activity, the products of their enzymatic degradation and the different enzymes of degradation and modification are considered.

[Aryl sulfatase of unusual specificity from the liver of marine mollusk Littorina kurila].

An aryl sulfatase of unusual specificity has been isolated from the liver of marine mollusk Littorina kurila. It hydrolyzes p-nitrophenyl sulfate, does not affect the natural fucoidan, and catalyzes splitting off of the sulfate group in position C4 of xylose residues within the carbohydrate chains of holostane triterpene glycosides from sea cucumbers. The properties of the enzyme were studied at pH 5.

[Metabolites of marine organisms as regulators of O-glycosylhydrolases].

The ability of metabolites contained in culture liquid of 62 strains of marine fungi to affect the activity of two digestive enzymes of marine mollusks--endo-1,3-beta-D-glucanase of Spisula sachalinensis and beta-D-glucosidase of Littorina kurila--was studied. It was found that 66 and 71% of specimens activated, 18 and 7% inhibited, and 16 and 22% did not affect the activity of endo-1,3-beta-D-glucanase and beta-D-glucosidase, respectively. It is demonstrated that the metabolites of brown algae and marine sponges can be used for a targeted regulation of enzyme biosynthesis by marine fungi.

Molecular cloning and characterization of an endo-1,3-beta-D-glucanase from the mollusk Spisula sachalinensis.

cDNA encoding the endo-1,3-beta-d-glucanase from Spisula sachalinensis (LIV) was amplified by PCR using oligonucleotides deduced from the N-terminal end peptide sequence. Predicted enzyme structure consists of 444 amino acids with a signal sequence. The mature enzyme has 316 amino acids and its deduced amino acid sequence coincides completely with the N-terminal end (38 amino acids) of the beta-1,3-glucanase (LIV) isolated from the mollusk.

Filamentous marine fungi as producers of O-glycosylhydrolases: beta-1,3-glucanase from Chaetomium indicum.

Ninety fungal strains (42 species) isolated from marine habitats were studied for their ability to produce extracellular enzymes. Cultural filtrates of these strains were shown to contain a series of glycosidases (beta-glucosidases, N-acetyl-beta-glucosaminidases, beta-galactosidases alpha-mannosidases) and glucanases (1,3-beta-glucanases, amylases) which varied with habitat. The level of activity depended on the species of fungi.

[O-glycosylhydrolases of marine filamentous fungi. beta-1,3-Glucanases of Trichoderma aureviride].

The ability to produce extracellular O-glycosylhydrolases was studied in 14 strains of marine filamentous fungi sampled from bottom sediments of the South China Sea. The following activities were detected in the culture liquids of the fungi: N-acetyl-D-glucosaminidase, D-glucosidase, D-galactosidase, beta-1,3-glucanase, amylase, and pustulanase. beta-1,3-Glucanases were isolated by ultrafiltration, hydrophobic interaction chromatography, and ion-exchange chromatography, and their properties were studied.

Beta-1,3-glucanase from unfertilized eggs of the sea urchin Strongylocentrotus intermedius. Comparison with beta-1,3-glucanases of marine and terrestrial mollusks.

beta-1,3-Glucanase (Lu) was isolated from unfertilized eggs of the sea urchin Strongylocentrotus intermedius. A comparative study of some properties of beta-1,3-glucanase Lu and beta-1,3-glucanases with different action types--endo-beta-1,3-glucanase from crystalline style of the marine mollusk Spisula sachalinensis (LIV) and exo-beta-1,3-glucanase from the terrestrial snail Eulota maakii (LII)--was performed. It was found that beta-1,3-glucanase Lu hydrolyzes laminaran with a high yield of glucose in the reaction products.

Distribution of O-glycosylhydrolases in marine invertebrates. Enzymes of the marine mollusk Littorina kurila that catalyze fucoidan transformation.

The distribution of O-glycosylhydrolases (fucoidan hydrolases, alpha-D-mannosidases, beta-D-glucosidases, and beta-D-galactosidases) in 30 species of marine invertebrates occurring in the Sea of Japan was studied. It is shown that fucoidanases and glycosidases are widespread in the animals analyzed. Some molluscan, annelid, and echinoderm species can probably serve as objects for isolation and detailed study of the fucoidan-hydrolyzing enzymes.

Brown seaweed protein as an inhibitor of marine mollusk endo-(1-->3)-beta-D-glucanases.

Aqueous ethanol extracts from brown seaweed were found to contain substances inhibiting endo-(1-->3)-beta-D-glucanases, the digestive enzymes of marine mollusks. The inhibitors were detected in 70% of the brown seaweeds investigated. An irreversible protein inhibitor with high specificity for endo-(1-->3)-beta-D-glucanases of marine mollusks was isolated from the brown seaweed, Laminaria cichorioides.

Proteins of brown seaweeds as inhibitors of endo-1-->3-beta-D-glucanases of marine invertebrates.

It has been found that aqueous-ethanol extracts of brown seaweeds contain substances inhibiting endo-1-->3-beta-D-glucanases, the digestive enzymes of marine mollusks. The inhibitors were detected in 14 of 21 brown seaweeds investigated. An irreversible protein inhibitor possessing high specificity toward endo-1-->3-beta-D-glucanases of marine mollusks was isolated from the brown seaweed Laminaria cichorioides.

Enzymes of carbohydrate metabolism of mycelial fungi from marine environments. beta-1,3-glucanase of the marine fungus Chaetomium indicum.

Thirty samples of fungi belonging to 17 species living in marine environments were studied for their ability to produce extracellular enzymes. In the culture fluids, a variety of glycosidases (beta-glucosidases, N-acetyl-beta-glucosaminidase, beta-galactosidases, and alpha-mannosidases) and glucanases (amylases and beta-1,3-glucanases) were found. Several cultures were found that could be used as efficient producers of either individual enzymes or a whole complement of enzymes degrading carbohydrate-containing compounds.

Alpha-galactosidase of the marine bacterium Pseudoalteromonas sp. KMM 701.

An alpha-galactosidase that inactivates the group specificity of B erythrocytes (group III) of human blood and does not affect A erythrocytes (group II) was isolated from the marine bacterium Pseudoalteromonas sp. KMM 701. The enzyme preparation did not contain lectin, hemolytic, sialidase, endoglycanase, or glycosidase activities.

Poly(A)-containing RNA in early embryogenesis of sea urchins.

The content, biosynthesis and template activity of poly(A)+ RNA in the early stages of sea urchin development have been studied. The amount of poly(A)+ RNA reaches a maximum at the middle blastula stage in polyribosomes and at the 8-blastomere stage in the cytoplasm. Poly(A)+ RNA synthesis becomes noticeable at the 64-blastomere stage and the spectrum of newly synthesized molecules is different from that at the middle blastula stage.

[Chemical modification of lysine residues of beta-1,3-glucanase from Spisula sachalinensis].

The effects of chemical modification of the amino groups of lysine residues on the activity of beta-1.3-glucanase from Spisula sachalinensis were studied. Modification of two lysine residues per molecule did not affect either the enzyme activity with respect to laminarine, nor the Km value.