Ginsenoside Compound K Production from Ginseng Root Extract by a Thermostable β-Glycosidase from<i>Sulfolobus solfataricus</i>

Noh, Kyeong-Hwan; Son, Ju-Wan; Kim, Hye-Jung; Oh, Deok‐Kun

doi:10.1271/bbb.80525

Cited by 116 publications

(70 citation statements)

References 20 publications

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“…The preferential reactivity of BgpA toward these three glucose moieties of Rb1 could be deduced from the Rb1 biotransformation pathway: i.e., Rb1 3 Gyp XVII 3 Gyp LXXV 3 C-K. BgpA preferred the outer glucose at position C-3, followed by the inner glucose at position C-3, and finally the outer glucose at position C-20. By comparison, family 1 ginsenoside-hydrolyzing glycosidases preferentially hydrolyze the outer glucose at position C-20 (16,28).…”

Section: Resultsmentioning

confidence: 99%

“…For example, a ␤-glucosidase isolated from a fungus converts Rb1 to C-K [20- (34). Two recombinant enzymes that convert major ginsenosides into rare ginsenosides have been cloned and expressed in Escherichia coli: Solfolobus solfataricus ␤-glycosidase, which transforms Rb1 or Rc to C-K (28), and ␤-glucosidase from a soil metagenome, which transforms Rb1 to Rd (16). Both of these glycoside hydrolases are family 1 glycoside hydrolases.…”

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confidence: 99%

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Identification and Characterization of a NovelTerrabacter ginsenosidimutanssp. nov. β-Glucosidase That Transforms Ginsenoside Rb1 into the Rare Gypenosides XVII and LXXV

Cui

Lee

et al. 2010

Appl Environ Microbiol

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Identification and Characterization of a NovelTerrabacter ginsenosidimutanssp. nov. β-Glucosidase That Transforms Ginsenoside Rb1 into the Rare Gypenosides XVII and LXXV

Cui

Lee

et al. 2010

Appl Environ Microbiol

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“…The minor deglycosylated ginsenosides are more pharmaceutically active than the major glycosylated ginsenosides because of higher bioavailability due to their smaller size and better permeability across the cell membrane (Kim et al 2005). Therefore, many studies have focused on the production of deglycosylated ginsenosides by hydrolyzing the sugar moieties in the glycosylated major ginsenosides by heating (Kim et al 2000), acid treatment (Bae et al 2004), fermentation (Zhou et al 2008), and enzymatic conversion methods (Noh et al 2009). Among these methods, enzymatic conversion is the Electronic supplementary material The online version of this article (doi:10.1007/s00253-015-6549-6) contains supplementary material, which is available to authorized users.…”

Section: Introductionmentioning

confidence: 99%

An amino acid at position 512 in β-glucosidase from Clavibacter michiganensis determines the regioselectivity for hydrolyzing gypenoside XVII

Shin

Hong

Seo

et al. 2015

Appl Microbiol Biotechnol

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A recombinant β-glucosidase from Clavibacter michiganensis specifically hydrolyzed the outer and inner glucose linked to the C-3 position in protopanaxadiol (PPD)-type ginsenosides and the C-6 position in protopanaxatriol (PPT)-type ginsenosides except for the hydrolysis of gypenoside LXXV (GypLXXV). The enzyme converted gypenoside XVII (GypXVII) to GypLXXV by hydrolyzing the inner glucose linked to the C-3 position. The substrate-binding residues obtained from the GypXVII-docked homology models of β-glucosidase from C. michiganensis were replaced with alanine, and the amino acid residue at position 512 was selected because of the changed regioselectivity of W512A. Site-directed mutagenesis for the amino acid residue at position 512 was performed. W512A and W512K hydrolyzed the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position of GypXVII to produce GypLXXV and F2. W512R hydrolyzed only the outer glucose linked to the C-20 position of GypXVII to produce F2. However, W512E and W512D exhibited no activity for GypXVII. Thus, the amino acid at position 512 is a critical residue to determine the regioselectivity for the hydrolysis of GypXVII. These wild-type and variant enzymes produced diverse ginsenosides, including GypXVII, GypLXXV, F2, and compound K, from ginsenoside Rb1. To the best of our knowledge, this is the first report of the alteration of regioselectivity on ginsenoside hydrolysis by protein engineering.

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“…b-Glucosidase from this bacterium is a b-glycosidase, is a thermostable enzyme and has concomitant b-galactosidase and b-xylosidase activities due to its broad specificity (Nucci et al 1993). Thus, the b-glucosidase has been applied to the hydrolysis of phytochemicals such as oleuropein and ginsenoside (Briante et al 2000;Noh et al 2009). …”

Section: Introductionmentioning

confidence: 99%

Characterization of a β-glucosidase from Sulfolobus solfataricus for isoflavone glycosides

et al. 2011

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The specific activity of a recombinant β-glucosidase from Sulfolobus solfataricus for isoflavones was: daidzin > glycitin > genistin > malonyl genistin > malonyl daidzin > malonyl glycitin. The hydrolytic activity of this enzyme for daidzin was highest at pH 5.5 and 90°C with a half-life of 18 h, a K (m) of 0.5 mM, and a k (cat) of 2532 s(-1). The enzyme converted 1 mM daidzin to 1 mM daidzein after 1 h with a molar yield of 100% and a productivity of 1 mM h(-1). Among β-glucosidases, that from S. solfataricus β had the highest thermostability, k (cat), k (cat)/K (m), conversion yield, and productivity in the hydrolysis of daidzin.

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Ginsenoside Compound K Production from Ginseng Root Extract by a Thermostable β-Glycosidase fromSulfolobus solfataricus

Cited by 116 publications

References 20 publications

Identification and Characterization of a NovelTerrabacter ginsenosidimutanssp. nov. β-Glucosidase That Transforms Ginsenoside Rb1 into the Rare Gypenosides XVII and LXXV

Identification and Characterization of a NovelTerrabacter ginsenosidimutanssp. nov. β-Glucosidase That Transforms Ginsenoside Rb1 into the Rare Gypenosides XVII and LXXV

An amino acid at position 512 in β-glucosidase from Clavibacter michiganensis determines the regioselectivity for hydrolyzing gypenoside XVII

Characterization of a β-glucosidase from Sulfolobus solfataricus for isoflavone glycosides

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