Release of Soybean Isoflavones by Using a β‐Glucosidase from Alicyclobacillus herbarius

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 heterologo...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2021-04, Vol.22 (7), p.1223-1231
Main Authors: Delgado, Lidia, Heckmann, Christian M., Di Pisa, Flavio, Gourlay, Louise, Paradisi, Francesca
Format: Article
Language:English
Subjects:
Alicyclobacillus - enzymology
Alicyclobacillus herbarius
beta-Glucosidase - chemistry
beta-Glucosidase - genetics
beta-Glucosidase - metabolism
biocatalysis
Catalytic Domain
Dietary supplements
E coli
Enzyme Stability
Enzymes
Escherichia coli - metabolism
Ethanol
extremophiles
Food conversion
Food industry
Food processing industry
Glucose
Glucose tolerance
Glucosidase
Glucosides
Glycine max - chemistry
Glycine max - metabolism
Glycosidases
Glycosides - metabolism
Hydrogen-Ion Concentration
hydrolases
Hydrolysis
Isoflavones
Isoflavones - chemistry
Isoflavones - metabolism
Kinetics
Organic solvents
Protein Structure, Tertiary
soy
Soybeans
Sugar
Temperature
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Summary: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. Tough guy: Enzymatic characterisation showed that a β‐glycosidase from Alicyclobacillus herbarius was stable over a broad range of pH values and temperatures, also exhibiting excellent tolerance to sugars and organic solvents, specially to ethanol. The enzyme was applied in the hydrolysis of isoflavone glucosides in an ethanolic extract of soy flour with outstanding results.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.202000688