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

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.

Producing natural vanilla extract from green vanilla beans using a β-glucosidase from Alicyclobacillus acidiphilus

“…Several β-glucosidases from the genus Alicyclobacillus with similar stability, co-solvent tolerance, and lack of glucose inhibition have previously been reported (Cao et al, 2018a;Delgado et al, 2020a;Di Lauro et al, 2006).…”

Alkaline–Enzymatic Hydrolysis for Improved Quantitation of Total Isoflavones in Soy Protein-Based Infant Food by UPLC–MS/MS

“…Most studies on β-glucosidase have focused on topics such as hydrolysis enhancement and enzyme immobilization for industrial applications. Some novel β-glucosidases have also been developed for this purpose. , However, these β-glucosidases are limited to a few glucoside ISFs, and data on malonyl and acetyl glucosides are lacking. To systemically evaluate the application of β-glucosidase in ISF determination, three commercial β-glucosidases were selected to hydrolyze malonyl and acetyl glucoside ISFs using enzymes from almonds, P.…”

Efficient 2-Step Enzymatic Cascade for the Bioconversion of Oleuropein into Hydroxytyrosol

“…Enzyme preparation including protein expression and purification were performed as previously described by Delgado et al 2021 [ 21 ]. Ahe has been expressed in very good yield (70–100 mg/L of culture), and analyzed by SDS page (See Supplementary Information, Figure S1 ).…”

“…In particular, a 2-step regioselective hydrolysis of OLE has been performed. HT has been obtained in high yields and rapid reaction times employing a halo-thermophilic β-glucosidase from Alicyclobacillus herbarius (Ahe) [ 21 ], which is able to cleave the glycosidic bond releasing GLU and OLE aglycone, followed by an acyl transferase from Mycobacterium smegmatis (MsAcT) [ 22 , 23 , 24 , 25 , 26 ], here exploited for its hydrolytic activity. The superior radical scavenging capacity of HT has been finally evaluated with respect to OLE parent compound and OLE aglycone through DPPH assay.…”