ArticleChembiochem : a European journal of chemical biology2021
Release of Soybean Isoflavones by Using a β-Glucosidase from Alicyclobacillus herbarius.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Characterization of a Novel GH3 β-Glucosidase with Alkali-Tolerant and Halophilic Properties from Pontixanthobacter luteolus SW-109.Applied biochemistry and biotechnology · 2026Article
- Production of soy aglycones as an alternative estrogen via innovative synergy of commercial and novelFood chemistry: X · 2025Article
- Valorization of Apple Pomace: Production of Phloretin Using a Bacterial Cellulose-Immobilized β-Glycosidase.ChemSusChem · 2025Article
- Enzymatic Deglycosylation and Lipophilization of Soy Glycosides into Value-Added Compounds for Food and Cosmetic Applications.ACS omega · 2025Article
- Effects of Soybean Extracts Prepared with BionurukPreventive nutrition and food science · 2025Article
- Efficient 2-Step Enzymatic Cascade for the Bioconversion of Oleuropein into Hydroxytyrosol.Antioxidants (Basel, Switzerland) · 2022Article
- Release of Soybean Isoflavones by Using a β-Glucosidase from Alicyclobacillus herbarius.Chembiochem : a European journal of chemical biology · 2021Article
- Production of Bovine Equol-Enriched Milk: A Review.Animals : an open access journal from MDPI · 2021Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
β-Glucosidases are used in the food industry to hydrolyse glycosidic bonds in complex sugars, with enzymes sourced from extremophiles better able to tolerate the process conditions. In this work, a novel β-glycosidase from the acidophilic organism Alicyclobacillus herbarius was cloned and heterologously expressed in Escherichia coli BL21(DE3). AheGH1 was stable over a broad range of pH values (5-11) and temperatures (4-55 °C). The enzyme exhibited excellent tolerance to fructose and good tolerance to glucose, retaining 65 % activity in the presence of 10 % (w/v) glucose. It also tolerated organic solvents, some of which appeared to have a stimulating effect, in particular ethanol with a 1.7-fold increase in activity at 10 % (v/v). The enzyme was then applied for the cleavage of isoflavone from isoflavone glucosides in an ethanolic extract of soy flour, to produce soy isoflavones, which constitute a valuable food supplement, full conversion was achieved within 15 min at 30 °C.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.