Improvement of isoflavone aglycones production using β-glucosidase secretory produced in recombinant Aspergillus oryzae

Horii, Ken; Adachi, Takashi; Matsuda, Tetsuya; Tanaka, Tsutomu; Sahara, Hiroshi; Shibasaki, Seiji; Ogino, Chiaki; Hata, Yutaka; Ueda, Mitsuyoshi; Kondo, Akihiko

doi:10.1016/j.molcatb.2008.11.013

Cited by 37 publications

(35 citation statements)

References 19 publications

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“…In contrast, enzymatic hydrolysis usually takes place at moderate pH and temperature and is an environmental-friendly process without generation of toxic or degraded products [21,22]. β-Glucosidase has been used for deglycosylation of isoflavone glucosides in soymilk into their aglycones [23] and for hydrolysis of resveratrol glucosides in wine in order to analyze the total wine resveratrol [24]. However, the high cost of β-glucosidase is the major concern of enzymatic transformation reactions for industrial applications.…”

Section: Introductionmentioning

confidence: 99%

Production of Resveratrol by Piceid Deglycosylation Using Cellulase

et al. 2016

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Abstract:Resveratrol is a dietary polyphenolic compound widely used in medicine, food, and cosmetic products. The glycoside form of resveratrol, piceid, is also present in several plant materials but is less bioavailable. In this study, enzymatic transformation of piceid into resveratrol using inexpensive cellulase was investigated. Response surface methodology was used to evaluate the effect of reaction parameters, including reaction temperature, reaction time, enzyme amount and pH. The optimal conditions for biotransformation of piceid to resveratrol are: a reaction temperature of 50˝C, reaction time of 4.75 h, enzyme amount of 2.5 fungal β-glucanase (FBG) units and pH of 4.3. In addition, the extracts from Polygonum cuspidatum root contained high amounts of piceid were treated with cellulase in order to deglycosylation that increased resveratrol yield. After treatment, the resveratrol yield significantly increased from 2.72 to 9.49 mg/g, while the piceid contents decreased from 8.60 to 0 mg/g. The result provides an efficient method to convert piceid in the extracts of P. cuspidatum root into resveratrol by cellulase.

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Section: Introductionmentioning

confidence: 99%

Production of Resveratrol by Piceid Deglycosylation Using Cellulase

et al. 2016

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“…By comparison, the At-Bgl had the second highest productivity for daidzein (1.14 mmol/(L·h)) and genistein (0.72 mmol/(L·h)), much higher than that of β-glucosidase from A.oryzae (Horii et al, 2009), soybean okara (Chiou et al, 2010), and Pyrococcus furiosus . In addition, the previously reported highest productivities for daidzein and genistein were 1.50 and 1.23 mmol/(L·h), respectively, produced by a β-glucosidase from Gongronella sp.…”

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

confidence: 91%

“…However, low solubility of isoflavones reduces the productivity of isoflavone aglycones in industrial production (Horii et al, 2009). To test the reactivity of At-Bgl toward isoflavone, the hydrolysis rate and the productivity were measured by HPLC using isoflavone flour extract as the substrate.…”

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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“…The strain A. oryzae niaD mutants harboring expression plasmid pISI-BGL1 (Horii et al 2009) were cultivated in 100 ml GPY medium [3% (w/v) glucose, 0.2% (w/v) KCl, 0.1% (w/v) KH 2 PO 4 , 0.05% (w/v) MgSO 4 Á 7H 2 O, 1% (w/v) peptone, and 0.5% (w/v) yeast extract, pH 6.0] at 30°C for 4 days and the mycelia were removed by filtration through a Myracloth (Calbiochem, La Jolla, CA, USA). After cultivation for 4 days, culture media containing b-glucosidase was filtered through a 0.45 lm PVDF filter unit to remove insoluble materials, and the filterate was concentrated using a centrifugal filter device (Millipore) with a 50,000 Da nominal molecular weight limit (NMWL).…”

Section: Yeast Strains and Growth Mediamentioning

confidence: 99%

Evaluation of cell surface-displayed protein stability against simulated gastric fluid

et al. 2009

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A molecular display technology that uses the displayed proteins on cell surfaces has many applications in microbiology and molecular biology. Here, we describe the resistance of displayed proteins to proteases using simulated gastric fluid (SGF), which included pepsin at pH 2. The displayed beta-glucosidase resisted pepsin digestion compared with secreted, free beta-glucosidase. In SDS-PAGE and Western blotting analysis, the secreted beta-glucosidase was immediately digested within 1 min following SGF treatment, although the displayed beta-glucosidase was stable for more than 60 min following SGF treatment. In addition, the residual activity of secreted beta-glucosidase was completely destroyed after 10 min SGF treatment. However, displayed beta-glucosidase retained 14% of its residual activity following the same treatment. These results clearly show that cell surface display technology using enzymes can reveal the protease resistance of a protein of interest under various conditions.

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Improvement of isoflavone aglycones production using β-glucosidase secretory produced in recombinant Aspergillus oryzae

Cited by 37 publications

References 19 publications

Production of Resveratrol by Piceid Deglycosylation Using Cellulase

Production of Resveratrol by Piceid Deglycosylation Using Cellulase

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

Evaluation of cell surface-displayed protein stability against simulated gastric fluid

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