6YN7

Crystal Structure of AHE enzyme from Alicyclobacillus herbarius

6YN7 の概要

• エントリーDOI: 10.2210/pdb6yn7/pdb
• 分子名称: AHE, beta-glucosidase enzyme, 1,2-ETHANEDIOL, NICKEL (II) ION, ... (6 entities in total)
• 機能のキーワード: ahe, alicyclobacillus herbarius, beta-glucosidase, hydrolase
• 由来する生物種: Alicyclobacillus herbarius
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 208542.84

構造登録者

Gourlay, L.J.,Di Pisa, F. (登録日: 2020-04-11, 公開日: 2021-02-03, 最終更新日: 2024-01-24)

主引用文献

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

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: 33237595
DOI: 10.1002/cbic.202000688

実験手法

X-RAY DIFFRACTION (1.98 Å)