ArticleJournal of Zhejiang University. Science. B2016
Characterization of β-glucosidase from Aspergillus terreus and its application in the hydrolysis of soybean isoflavones.
Article in Journal of Zhejiang University. Science. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 33 citations in OpenAlex.
- The role of gut mycobiome in responses to cancer immunotherapy.Gut microbes · 2025Review
- A thermostable and inhibitor resistant β-glucosidase from Rasamsonia emersonii for efficient hydrolysis of lignocellulosics biomass.Bioprocess and biosystems engineering · 2024Article
- Enzymatic Activity and Amino Acids Production of Predominant Fungi from Traditional Meju during Soybean Fermentation.Journal of microbiology and biotechnology · 2024Article
- Mycotransformation of Commercial Grade Cypermethrin Dispersion byMolecules (Basel, Switzerland) · 2024Article
- Soybean (3 Biotech · 2023Article
- Highly Efficient Biotransformation of Phenolic Glycosides Using a Recombinant βFrontiers in microbiology · 2022Article
- Isolation ofFoods (Basel, Switzerland) · 2019Article
- Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application.Biomolecules · 2019Review
- A Biotransformation Process for Production of Genistein from Sophoricoside by a Strain of Rhizopus oryza.Scientific reports · 2019Article
- Synchronized purification and immobilization of his-tagged β-glucosidase via FeScientific reports · 2017Article
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6 authors at 1 institution in 1 country.
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Abstract
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-of-flight/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 Km (apparent Michaelis-Menten constant) and Vmax (maximal reaction velocity) for p-nitrophenyl-β-D-glucopyranoside (pNPG) were 1.73 mmol/L and 42.37 U/mg, respectively. The Km and Vmax 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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