ArticleJournal of industrial microbiology & biotechnology2018
A highly glucose-tolerant GH1 β-glucosidase with greater conversion rate of soybean isoflavones in monogastric animals.
Article in Journal of industrial microbiology & biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Temperature-Dependent Conformational Dynamics of Substrate Entrance Loops in β-Glucosidase: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Efficient Biotransformation of Icariin to Baohuoside I Using Two Novel GH1 β-Glucosidases.Molecules (Basel, Switzerland) · 2024Article
- Characterization of a Novel Hyperthermophilic GH1 β-Glucosidase fromMicroorganisms · 2024Article
- Characterization of a novel cold-adapted GH1 β-glucosidase fromCurrent research in food science · 2024Article
- Characterization of a novel recombinant halophilic β-glucosidase of Trichoderma harzianum derived from Hainan mangrove.BMC microbiology · 2022Article
- Release of Soybean Isoflavones by Using a β-Glucosidase from Alicyclobacillus herbarius.Chembiochem : a European journal of chemical biology · 2021Article
- Metagenomic Insights Into the Taxonomic and Functional Features ofFrontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the feed industry, β-glucosidase has been widely used in the conversion of inactive and bounded soybean isoflavones into active aglycones. However, the conversion is frequently inhibited by the high concentration of intestinal glucose in monogastric animals. In this study, a GH1 β-glucosidase (AsBG1) with high specific activity, thermostability and glucose tolerance (IC
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Registered trials
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