A β-Rutinosidase from<i>Penicillium rugulosum</i>IFO 7242 That Is a Peculiar Flavonoid Glycosidase

Narikawa, Tatsuya; Shinoyama, Hirofumi; Fujii, Tomoyuki

doi:10.1271/bbb.64.1317

Cited by 47 publications

(38 citation statements)

References 12 publications

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“…Three were shown to be exclusively specific for 3-O-linked rutinosides. [13][14][15] In contrast to these, the extracellular a-l-rhamnosyl-b-d-glucosidase from Acremonium sp. was solely active on 7-Olinked rutinosides such as hesperidin, and did not accept rutin as a substrate.…”

Section: Expression and Purification Of Recombinant Rutinosidasementioning

confidence: 99%

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

et al. 2014

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Abstract:We report the first heterologous production of a fungal rutinosidase (6-O-a-l-rhamnopyranosyl-b-d-glucopyranosidase) in Pichia pastoris. The recombinant rutinosidase was purified from the culture medium to apparent homogeneity and biochemically characterized. The enzyme reacts with rutin and cleaves the glycosidic linkage between the disaccharide rutinose and the aglycone. Furthermore, it exhibits high transglycosylation activity, transferring rutinose from rutin as a glycosyl donor onto various alcohols and phenols. The utility of the recombinant rutinosidase was demonstrated by its use for the synthesis of a broad spectrum of rutinosides of primary (saturated and unsaturated), secondary, acyclic and phenolic alcohols as well as for the preparation of free rutinose. Moreover, the a-l-rhamnosidase-catalyzed synthesis of a chromogenic substrate for a rutinosidase assay -para-nitrophenyl b-rutinoside -is described.

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Section: Expression and Purification Of Recombinant Rutinosidasementioning

confidence: 99%

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

et al. 2014

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“…Gü nata et al (1998) have also detected and identified an enzyme having ␤-primeverosidase-and/or rutinase-like activity from grape (Vitis vinifera) berry peels. Although some of diglycosidases have been purified from plants (Imaseki and Yamamoto, 1961;Lizotte and Poulton, 1988;Yasuda and Nakagawa, 1994) and also from microorganisms (Narikawa et al, 2000;Yamamoto et al, 2002), they have never been characterized in molecular levels. In this paper, we confirmed the tea leaf ␤-primeverosidase as a unique diglycosidase by purification from tea leaves and cloning of the cDNA encoding the enzyme.…”

Section: Distribution Of the ␤-Primeverosidase In Tea Shootsmentioning

confidence: 99%

Cloning of β-Primeverosidase from Tea Leaves, a Key Enzyme in Tea Aroma Formation

et al. 2002

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A ␤-primeverosidase from tea (Camellia sinensis) plants is a unique disaccharide-specific glycosidase, which hydrolyzes aroma precursors of ␤-primeverosides (6-O-␤-d-xylopyranosyl-␤-d-glucopyranosides) to liberate various aroma compounds, and the enzyme is deeply concerned with the floral aroma formation in oolong tea and black tea during the manufacturing process. The ␤-primeverosidase was purified from fresh leaves of a cultivar for green tea (C. sinensis var sinensis cv Yabukita), and its partial amino acid sequences were determined. The ␤-primeverosidase cDNA has been isolated from a cDNA library of cv Yabukita using degenerate oligonucleotide primers. The cDNA insert encodes a polypeptide consisting of an N-terminal signal peptide of 28 amino acid residues and a 479-amino acid mature protein. The ␤-primeverosidase protein sequence was 50% to 60% identical to ␤-glucosidases from various plants and was classified in a family 1 glycosyl hydrolase. The mature form of the ␤-primeverosidase expressed in Escherichia coli was able to hydrolyze ␤-primeverosides to liberate a primeverose unit and aglycons, but did not act on 2-phenylethyl ␤-d-glucopyranoside. These results indicate that the ␤-primeverosidase selectively recognizes the ␤-primeverosides as substrates and specifically hydrolyzes the ␤-glycosidic bond between the disaccharide and the aglycons. The stereochemistry for enzymatic hydrolysis of 2-phenylethyl ␤-primeveroside by the ␤-primeverosidase was followed by 1 H-nuclear magnetic resonance spectroscopy, revealing that the enzyme hydrolyzes the ␤-primeveroside by a retaining mechanism. The roles of the ␤-primeverosidase in the defense mechanism in tea plants and the floral aroma formation during tea manufacturing process are also discussed.

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“…Moreover, the rutin degrade enzyme of P. glucanolyticus D3 is produced constitutively, contrasting to the reported enzymes of Aspergillus, Penicillum, Thermoactinomyces and Streptococcus, which are induced rutin degrade enzymes of different types (Krishnamurty et al, 1970;Narikawa et al, 2000;Yang et al, 2009;Mamma et al, 2004). This characteristic enables P. glucanolyticus D3 with lower cost in enzyme production.…”

Section: Discussionmentioning

confidence: 92%

“…It had been reported that rutin could be degraded by microorganisms, such as Aspergihs flavus (Krishnamurty et al, 1970), Penicillum rugulosum (Narikawa et al, 2000) and Thermoactinomyces vulgaris (Yang et al, 2009), and so on. These microorganisms produced β-glucosidases which converted rutin (quercetin-3-O-β-D-glucose-α-L-rhamnose) to quercetin.…”

mentioning

confidence: 99%

Screening and Identification of a Quercetin-Producing Bacterium Paenibacillus glucanolyticu D3

Lu¹,

Zhang²,

Song³

2012

ENRR

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Quercetin is a kind of flavonoid, which has outstanding drug action. To develop the production technology of quercetin by microorganism, strains that can transform rutin to quercetin were isolated from soil, screened by TLC and re-screened by HPLC. As a result, strain D3 with the highest transformation ability was obtained. The hydrolyze enzyme was intracellular enzyme and transformation rate was 41.6% within a system comprising of 50mg wet cells in 4mL of 0.1% rutin solution and transformed for 72hr at 25°C. Strain D3 was identified as Paenibacillus glucanolyticus by integrating the 16S rDNA phylogeny analysis result and a variety of morphological, physiological and biochemical features.

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A β-Rutinosidase fromPenicillium rugulosumIFO 7242 That Is a Peculiar Flavonoid Glycosidase

Cited by 47 publications

References 12 publications

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

Cloning of β-Primeverosidase from Tea Leaves, a Key Enzyme in Tea Aroma Formation

Screening and Identification of a Quercetin-Producing Bacterium Paenibacillus glucanolyticu D3

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