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

Kim, Bi-Na; Yeom, Soo‐Jin; Kim, Yeong-Su; Oh, Deok‐Kun

doi:10.1007/s10529-011-0739-9

Cited by 41 publications

(26 citation statements)

References 18 publications

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“…The enzymatic methods are considered as the most promising approach with advantages of fewer byproducts, superior environmental protection, and better stereo-specificity [15]. In particular, the purified recombinant enzymes exhibit higher selectivity and efficiency than those isolated and purified from cultured microorganisms [16].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Biotransformation of Ginsenoside Rb1 and Gypenoside XVII into Ginsenosides Rd and F2 by Recombinant β-glucosidase from Flavobacterium johnsoniae

Hong

Cui

Kim³

et al. 2012

Journal of Ginseng Research

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This study focused on the enzymatic biotransformation of the major ginsenoside Rb1 into Rd for the mass production of minor ginsenosides using a novel recombinant β-glucosidase from Flavobacterium johnsoniae. The gene (bglF3) consisting of 2,235 bp (744 amino acid residues) was cloned and the recombinant enzyme overexpressed in Escherichia coli BL21(DE3) was characterized. This enzyme could transform ginsenoside Rb1 and gypenoside XVII to the ginsenosides Rd and F2, respectively. The glutathione S-transferase (GST) fused BglF3 was purified with GST-bind agarose resin and characterized. The kinetic parameters for β-glucosidase had apparent Km values of 0.91±0.02 and 2.84±0.05 mM and Vmax values of 5.75±0.12 and 0.71±0.01 μmol·min-1·mg of protein-1 against p-nitrophenyl-β-D-glucopyranoside and Rb1, respectively. At optimal conditions of pH 6.0 and 37℃, BglF3 could only hydrolyze the outer glucose moiety of ginsenoside Rb1 and gypenoside XVII at the C-20 position of aglycon into ginsenosides Rd and F2, respectively. These results indicate that the recombinant BglF3 could be useful for the mass production of ginsenosides Rd and F2 in the pharmaceutical or cosmetic industry.

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Section: Introductionmentioning

confidence: 99%

Enzymatic Biotransformation of Ginsenoside Rb1 and Gypenoside XVII into Ginsenosides Rd and F2 by Recombinant β-glucosidase from Flavobacterium johnsoniae

Hong

Cui

Kim³

et al. 2012

Journal of Ginseng Research

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“…Numerous studies on GHs have been performed in bacteria, plants and fungi (Yang et al ., ; Yin et al ., ; Chuankhayan et al ., ; Kaya et al ., ; Kuo & Lee, ; Choi et al ., ; Hu et al ., ; Xue et al ., ; Kim et al ., , ; Song et al ., ; Li et al ., ; Sakurama et al ., ). However, our understanding of β‐glucosidases from B. thetaiotaomicron remains limited.…”

Section: Discussionmentioning

confidence: 99%

“…However, absorption is increased upon release of the sugar moiety from isoflavone glycosides (Izumi et al ., ; Setchell et al ., ; Kim et al ., ; Yin et al ., ; Ismail & Hayes, ; Chuankhayan et al ., ; Kaya et al ., ; Kuo & Lee, ; Hu et al ., ; Xue et al ., ,b; Yang et al ., ; Song et al ., ). Because of the in vivo roles of highly bioactive isoflavones, many studies have examined the conversion of isoflavone glycosides into their aglycones and physiological components (Izumi et al ., ; Jenkins et al ., ; Setchell et al ., ; Yang et al ., , ; Ismail & Hayes, ; Chuankhayan et al ., ; Kaya et al ., ; Kuo & Lee, ; Hu et al ., ; Xue et al ., ,b; Kim et al ., , ; Song et al ., ; Li et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Properties and applications of β‐glycosidase from Bacteroides thetaiotaomicron that specifically hydrolyses isoflavone glycosides

Byun

Choi

Lee

et al. 2015

Int J of Food Sci Tech

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To modify the glycan part of glycosides, the gene encoding b-glycosidase was cloned from Bacteroides thetaiotaomicron VPI-5482. The cloned gene, bt_1780, was expressed in Escherichia coli MC1061 and the expressed enzyme was purified using Ni-NTA affinity chromatography. The purified enzyme, BTBG, showed optimal activity at 50°C and pH 5.5. Interestingly, this enzyme did not have any hydrolysing activity on ordinary b-linkage-containing substrates such as xylobiose, lactose and cello-oligosaccharide, but specifically hydrolysed isoflavone glycosides such as daidzin, genistin and glycitin. Compared to a commercial beta glucosidase, BTBG selectively hydrolysed isoflavone glycosides in soybean extract mixture solution. These results suggest that BTBG may be a specialized enzyme for the hydrolysis of glycosides and that the substrate specificity of BTBG is applicable for the bioconversion of isoflavone glycosides in the food industry.

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“…Enzymatic hydrolysis of β-glucosidase towards soybean isoflavone is an important application in the food and feed industry, which has been investigated by direct use of β-glucosidase from plants and microorganisms (Chuankhayan et al, 2007;Kaya Yang et al, 2009;Song et al, 2011;Kim et al, 2012;Fang et al, 2014;Fujita et al, 2015). However, low solubility of isoflavones reduces the productivity of isoflavone aglycones in industrial production (Horii et al, 2009).…”

Section: Hydrolysis Of Soybean Isoflavone By a Terreus β-Glucosidasementioning

confidence: 99%

Characterization of β-glucosidase from Aspergillus terreus and its application in the hydrolysis of soybean isoflavones

Yan

Xia

Zhang

et al. 2016

J. Zhejiang Univ. Sci. B

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An extracellular β-glucosidase produced by Aspergillus terreus was identified, purified, characterized and was tested for the hydrolysis of soybean isoflavone. Matrix-assisted laser desorption/ionization with tandem time-offlight/time-of-flight mass spectrometry (MALDI-TOF/TOF MS) revealed the protein to be a member of the glycosyl hydrolase family 3 with an apparent molecular mass of about 120 kDa. The purified β-glucosidase showed optimal activity at pH 5.0 and 65 °C and was very stable at 50 °C. Moreover, the enzyme exhibited good stability over pH 3.0-8.0 and possessed high tolerance towards pepsin and trypsin. The kinetic parameters K m (apparent MichaelisMenten constant) and V max (maximal reaction velocity) for p-nitrophenyl-β-D-glucopyranoside (pNPG) were 1.73 mmol/L and 42.37 U/mg, respectively. The K m and V max for cellobiose were 4.11 mmol/L and 5.7 U/mg, respectively. The enzyme efficiently converted isoflavone glycosides to aglycones, with a hydrolysis rate of 95.8% for daidzin, 86.7% for genistin, and 72.1% for glycitin. Meanwhile, the productivities were 1.14 mmol/(L·h) for daidzein, 0.72 mmol/(L·h) for genistein, and 0.19 mmol/(L·h) for glycitein. This is the first report on the application of A. terreus β-glucosidase for converting isoflavone glycosides to their aglycones in soybean products.

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

Cited by 41 publications

References 18 publications

Enzymatic Biotransformation of Ginsenoside Rb1 and Gypenoside XVII into Ginsenosides Rd and F2 by Recombinant β-glucosidase from Flavobacterium johnsoniae

Enzymatic Biotransformation of Ginsenoside Rb1 and Gypenoside XVII into Ginsenosides Rd and F2 by Recombinant β-glucosidase from Flavobacterium johnsoniae

Properties and applications of β‐glycosidase from Bacteroides thetaiotaomicron that specifically hydrolyses isoflavone glycosides

Characterization of β-glucosidase from Aspergillus terreus and its application in the hydrolysis of soybean isoflavones

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