A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner

Suzuki, Harumasa; Suzuki, Ken-ichi; Inoue, Akira; Ojima, Takao

doi:10.1016/j.carres.2006.04.032

Cited by 100 publications

(81 citation statements)

References 35 publications

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“…Biochemical properties of sea hare mannosidase will be published elsewhere. On the other hand, we have reported various kinds of molluscan polysaccharidedegrading enzymes, e.g., alginate lyase, cellulase, and -1,3-glucanase (Shimizu et al, 2003;Suzuki et al, 2003;Suzuki et al, 2006;Hata et al, 2009;Kumagai and Ojima, 2010). Studies on these enzymes are expected to provide us the useful information about the degradation process of seaweeds' polysaccharides, which are expected as functional polysaccharides for human and a potential biomass in future.…”

Section: Discussionmentioning

confidence: 99%

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

Zahura¹,

Rahman²,

Inoue³

et al. 2010

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Section: Discussionmentioning

confidence: 99%

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

Zahura¹,

Rahman²,

Inoue³

et al. 2010

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…13 A number of alginate lyases have been identified, cloned, purified and characterized from various sources, [14][15][16][17][18] including marine and terrestrial bacteria, marine mollusks and algae. They can be classed into 2 groups due to their substrate specificities, 13 molecular weights 19 and action modes.…”

Section: Introductionmentioning

confidence: 99%

Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications

2015

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A lginate lyases catalyze the degradation of alginate, a complex copolymer of a-L-guluronate and its C5 epimer b-D-mannuronate. The enzymes have been isolated from various kinds of organisms with different substrate specificities, including algae, marine mollusks, marine and terrestrial bacteria, and some viruses and fungi. With the progress of structural biology, many kinds of alginate lyases of different polysaccharide lyases families have been characterized by obtaining crystal structures, and the catalytic mechanism has also been elucidated. Combined with various studies, we summarized the source, classification and properties of the alginate lyases from different polysaccharide lyases families. The relationship between substrate specificity and protein sequence was also investigated.

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“…reported the presence of an exo type enzyme from the digestive fluid of abalone that could act not only on unsaturated trisaccharides but also on alginate and mannuronate rich polymers, producing only unsaturated disaccharides. 7) Furthermore, Miyake showed that cooperative actions of 4 alginate lyases caused the complete depolymerization of alginate in Sphingomonas sp. A1.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Alginate Lyase from Pseudoalteromonas sp. Strain No. 1786

茶木¹,

馬場²,

樋浦³

et al. 2008

J. Appl. Glycosci.

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Alginic acid is a natural acidic linear polysaccharide and the main component of brown algae which plays an important role in keeping seaweed flexible and its intercellular tissues strong. 1) It is composed of β D mannuronate (M) and α L guluronate (G), which are linked by (1 4) glycosidic bonds. Alginate may be organized in three ways: as homopolymeric M blocks, homopolymeric G blocks, or heteropolymeric M G blocks in random arrangements. The proportion of these blocks depends upon the source of the alginate, and varies in different parts of the algal tissue. 2) Alginates are widely used in foods, pharmaceuticals, and cosmetics as gelling agents, stabilizers, or agents providing high viscosity. 3) To date, many studies have been reported on alginate degrading enzymes that have been isolated from many sources, including brown algae, 4) mollusks 5 7) and marine bacteria. 8 14) It is well known that most enzymes are of the lyase type that degrade alginate polysaccharide by a β elimination mechanism, a double bond being formed between the C4 and C5 carbons at the non reducing terminal (4 deoxy α L erythro hex 4 enopyranosyluronic acid, ∆). 15) Alginate lyase is classified into two groups in the substrate specificity. One is poly(β D 1,4 mannuronate)lyase (EC 4.2.2.3) and the other is poly(α L 1,4 guluronate)lyase (EC 4.2.2.11).Previously, we found that a crude enzyme from a marine bacterium which catalyzed the degradation of alginate, resulted in alginate oligosaccharides. 16) However, only limited information has been reported about the bacterium and the enzyme. In the present study, we attempted to characterize the bacterium in detail. Moreover, the enzyme was purified by DEAE HPLC and some properties of the enzyme were studied. MATERIALS AND METHODS Materials.Sodium alginate (320 380 cps, 1% solution at 20 C, Kimica Corp., Kimitsu, Japan) was used as a carbon source. Poly β D mannuronate (PM) rich and poly α L guluronate (PG) rich solutions were prepared from the sodium alginate according to the method of Haug et al . 17) Other materials and reagents were commercially available.Bacterial strains and growth media. The bacterium (strain No. 1786) was isolated from the intestinal contents of an arthropod. The bacterium was maintained in medium composed of 1.00% sodium alginate, 1.00% Na2SO4, 0.08% KCl, 1.24% MgSO4, 0.01% K2HPO4, 0.10% NH4Cl, 0.01% ammonium ferric citrate, and 0.15% CaCl2. The bacterium was inoculated into 500 mL flasks containing 200 mL of the above medium, and grown at 25 C for 48 h.Classification of the marine bacterium. Classification of the strain No. 1786 bacterium was performed based on morphological, biochemical and physiological characteristics and 16S rDNA sequence. Phenotypic tests were performed as described by Barrow and Feltham. 18) We also performed biochemical characterization and utilization test using the API 20NE system (bioMerieux, Lyon, France). Abstract: High activity of alginate lyase was produced by a marine bacterium (strain No. 1786), which was isolated from the intesti...

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A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner

Cited by 100 publications

References 35 publications

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications

Purification and Characterization of Alginate Lyase from Pseudoalteromonas sp. Strain No. 1786

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