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

Delgado, Lidia; Heckmann, Christian M.; Di Pisa, Flavio; Gourlay, Louise; Paradisi, Francesca (2021). Release of Soybean Isoflavones by Using a β‐Glucosidase from Alicyclobacillus herbarius. ChemBioChem, 22(7), pp. 1223-1231. Wiley-VCH 10.1002/cbic.202000688

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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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