6YN7
Crystal Structure of AHE enzyme from Alicyclobacillus herbarius
Summary for 6YN7
| Entry DOI | 10.2210/pdb6yn7/pdb |
| Descriptor | AHE, beta-glucosidase enzyme, 1,2-ETHANEDIOL, NICKEL (II) ION, ... (6 entities in total) |
| Functional Keywords | ahe, alicyclobacillus herbarius, beta-glucosidase, hydrolase |
| Biological source | Alicyclobacillus herbarius |
| Total number of polymer chains | 4 |
| Total formula weight | 208542.84 |
| Authors | Gourlay, L.J.,Di Pisa, F. (deposition date: 2020-04-11, release date: 2021-02-03, Last modification date: 2024-01-24) |
| Primary citation | Delgado, L.,Heckmann, C.M.,Di Pisa, F.,Gourlay, L.,Paradisi, F. Release of Soybean Isoflavones by Using a beta-Glucosidase from Alicyclobacillus herbarius. Chembiochem, 22:1223-1231, 2021 Cited by PubMed 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. PubMed: 33237595DOI: 10.1002/cbic.202000688 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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