6yn7

Publication Abstract from PubMed

beta-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 beta-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 degrees 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 degrees C.

Release of Soybean Isoflavones by Using a beta-Glucosidase from Alicyclobacillus herbarius.,Delgado L, Heckmann CM, Di Pisa F, Gourlay L, Paradisi F Chembiochem. 2020 Nov 25. doi: 10.1002/cbic.202000688. PMID:33237595^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.