Endo-β-1,3-galactanase from Winter Mushroom Flammulina velutipes

Kotake, Toshihisa; Hirata, Naohiro; Degi, Yuta; Ishiguro, Maki; Kitazawa, Kiminari; Takata, Ryohei; Ichinose, Hitomi; Kaneko, Satoshi; Igarashi, Kiyohiko; Samejima, Masahiro; Tsumuraya, Yoichi

doi:10.1074/jbc.m111.251736

Cited by 40 publications

(31 citation statements)

References 48 publications

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“…Studies have also reported isolation of proteins such as hemagglutanin which has mitogenic and antiproliferative functions, ice binding proteins and also the flammutoxin as a cytolysin (Tadjibaeva et al, 2000; Ng et al, 2006; Raymond and Janech, 2009). In addition, proflamin, a glycoprotein enzyme with anticancer activity, and asparaginase were also discovered in the mycelium of the mushroom (Maruyama and Ikekawa, 2007; Eisele et al, 2011; Kotake et al, 2011). …”

Section: Chemical Composition and Nutritional Value Of F Velutipesmentioning

confidence: 99%

Golden Needle Mushroom: A Culinary Medicine with Evidenced-Based Biological Activities and Health Promoting Properties

et al. 2016

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Flammulina velutipes (enoki, velvet shank, golden needle mushroom or winter mushroom), one of the main edible mushrooms on the market, has long been recognized for its nutritional value and delicious taste. In recent decades, research has expanded beyond detailing its nutritional composition and delved into the biological activities and potential health benefits of its constituents. Many bioactive constituents from a range of families have been isolated from different parts of the mushroom, including carbohydrates, protein, lipids, glycoproteins, phenols, and sesquiterpenes. These compounds have been demonstrated to exhibit various biological activities, such as antitumour and anticancer activities, anti-atherosclerotic and thrombosis inhibition activity, antihypertensive and cholesterol lowering effects, anti-aging and antioxidant properties, ability to aid with restoring memory and overcoming learning deficits, anti-inflammatory, immunomodulatory, anti-bacterial, ribosome inactivation and melanosis inhibition. This review aims to consolidate the information concerning the phytochemistry and biological activities of various compounds isolated from F. velutipes to demonstrate that this mushroom is not only a great source of nutrients but also possesses tremendous potential in pharmaceutical drug development.

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Section: Chemical Composition and Nutritional Value Of F Velutipesmentioning

confidence: 99%

Golden Needle Mushroom: A Culinary Medicine with Evidenced-Based Biological Activities and Health Promoting Properties

et al. 2016

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“…On the contrary, b-galactans III and IV, which have a high proportion of b-1,3-galactan, exhibited significantly higher reactivity than native gum arabic and b-galactan I based on sugar weight. Yariv reactivity of b-galactan IV was lost by treatment with endo-b-1,3-galactanase from winter mushroom (Flammulina velutipes), FvEn3Gal (Kotake et al, 2011). b-Galactan IV also failed to interact with a-Gal-Yariv (Supplemental Fig.…”

Section: Effect Of the Removal Of B-16-galactan Side Chains On Yarivmentioning

confidence: 99%

“…The content of uronic acid was measured by a modified carbazole-sulfuric acid method (Galambos, 1967). In the hydrolysis of b-galactan IV and b-1,3-Gal 9 , recombinant FvEn3Gal was used (Kotake et al, 2011).…”

Section: Trimming Of Agpmentioning

confidence: 99%

β-Galactosyl Yariv Reagent Binds to the β-1,3-Galactan of Arabinogalactan Proteins

et al. 2013

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Yariv phenylglycosides [1,3,5-tri(p-glycosyloxyphenylazo)-2,4,6-trihydroxybenzene] are a group of chemical compounds that selectively bind to arabinogalactan proteins (AGPs), a type of plant proteoglycan. Yariv phenylglycosides are widely used as cytochemical reagents to perturb the molecular functions of AGPs as well as for the detection, quantification, purification, and staining of AGPs. However, the target structure in AGPs to which Yariv phenylglycosides bind has not been determined. Here, we identify the structural element of AGPs required for the interaction with Yariv phenylglycosides by stepwise trimming of the arabinogalactan moieties using combinations of specific glycoside hydrolases. Whereas the precipitation with Yariv phenylglycosides (Yariv reactivity) of radish (Raphanus sativus) root AGP was not reduced after enzyme treatment to remove a-L-arabinofuranosyl and b-glucuronosyl residues and b-1,6-galactan side chains, it was completely lost after degradation of the b-1,3-galactan main chains. In addition, Yariv reactivity of gum arabic, a commercial product of acacia (Acacia senegal) AGPs, increased rather than decreased during the repeated degradation of b-1,6-galactan side chains by Smith degradation. Among various oligosaccharides corresponding to partial structures of AGPs, b-1,3-galactooligosaccharides longer than b-1,3-galactoheptaose exhibited significant precipitation with Yariv in a radial diffusion assay on agar. A pull-down assay using oligosaccharides cross linked to hydrazine beads detected an interaction of b-1,3-galactooligosaccharides longer than b-1,3-galactopentaose with Yariv phenylglycoside. To the contrary, no interaction with Yariv was detected for b-1,6-galactooligosaccharides of any length. Therefore, we conclude that Yariv phenylglycosides should be considered specific binding reagents for b-1,3-galactan chains longer than five residues, and seven residues are sufficient for cross linking, leading to precipitation of the Yariv phenylglycosides.Arabinogalactan proteins (AGPs) are a type of plant proteoglycans consisting of a Hyp-rich core protein and large arabinogalactan (AG) moieties (Fincher et al., 1983;Nothnagel, 1997). Although there are many molecular species of AGP differentiated by their core proteins, the AG moieties commonly comprise b-1,3-galactan main chains and b-1,6-galactan side chains, to which L-Ara and other auxiliary sugars, such as GlcA, 4-O-methyl-GlcA, L-Fuc, L-Rha, and Xyl, are attached (Fincher et al., 1983;Nothnagel, 1997;Seifert and Roberts, 2007). A commercial product of AGPs prepared from the acacia (Acacia senegal) tree is known as gum arabic and utilized as a food stabilizer. In the Japanese herbal remedy Juzen-Taiho-To, AGs from Astragalus membranaceus are the active ingredient (Majewska-Sawka and Nothnagel, 2000;Kiyohara et al., 2002). In intact plants, AGPs are implicated in various physiological events and serve as extracellular constituents and signaling molecules. For instance, an AGP from stylar transmitting tissue attracts pollen tub...

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“…42,45,46 The CAZy database (http://www.cazy.org/) 50 classifies glycoyl hydrolases into 130 families based on amino acid sequence similarities. Recently, Kotake et al 40 reported on the isolation of an endo -β-(1→3)-Dgalactanase from the mushroom, Flammulina velutipes . Sequence information and phylogenetic analysis determined that this enzyme belongs to CAZy GH 16, a family containing other endo -acting enzymes, including endo -β-(1→3)- and endo -β-(1→3, 1→4)- glucanases.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, there is only one report to date of the isolation of an endo -β-(1→3)-D-galactanase. 40 Enzymes may have different modes of action and/or catalytic sites. It is therefore important to isolate a wide spectrum of hydrolytic enzymes that cleave specific glycosyl linkages of the type II AGs.…”

Section: Introductionmentioning

confidence: 99%

An exo-β-(1→3)-d-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure

Ling

Lee

Ellis

et al. 2012

Carbohydrate Research

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An exo-β-(1→3)-D-galactanase (SGalase1) that specifically cleaves the β-(1→3)-D-galactan backbone of arabinogalactan-proteins (AGPs) was isolated from culture filtrates of a soil Streptomyces sp. Internal peptide sequence information was used to clone and recombinantly express the gene in E. coli. The molecular mass of the isolated enzyme was ~45 kDa, similar to the 48.2 kDa mass predicted from the amino acid sequence. The pI, pH and temperature optima for the enzyme were ~7.45, 3.8 and 48 °C, respectively. The native and recombinant enzymes specifically hydrolysed β-(1→3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. A second homologous Streptomyces gene (SGalase2) was also cloned and expressed. SGalase2 was similar in size (47.9 kDa) and enzyme activity to SGalase1 but differed in its pH optimum (pH 5). Both SGalase1 and SGalase2 are predicted to belong to the CAZy glycosyl hydrolase family GH 43 based on activity, sequence homology and phylogenetic analysis. The Km and Vmax of the native exo-β-(1→3)-D-galactanase for de-arabinosylated gum arabic (dGA) were 19 mg/ml and 9.7 μmol D-Gal/min/mg protein, respectively. The activity of these enzymes is well suited for the study of type II galactan structures and provides an important tool for the investigation of the biological role of AGPs in plants. De-arabinosylated gum arabic (dGA) was used as a model to investigate the use of these enzymes in defining type II galactan structure. Exhaustive hydrolysis of dGA resulted in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating.

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Endo-β-1,3-galactanase from Winter Mushroom Flammulina velutipes

Cited by 40 publications

References 48 publications

Golden Needle Mushroom: A Culinary Medicine with Evidenced-Based Biological Activities and Health Promoting Properties

Golden Needle Mushroom: A Culinary Medicine with Evidenced-Based Biological Activities and Health Promoting Properties

β-Galactosyl Yariv Reagent Binds to the β-1,3-Galactan of Arabinogalactan Proteins

An exo-β-(1→3)-d-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure

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