A β-glucosidase from Novosphingobium sp GX9 with high catalytic efficiency toward isoflavonoid glycoside hydrolysis and (+)-catechin transglycosylation
A β-glucosidase from Novosphingobium sp GX9 with high catalytic efficiency toward isoflavonoid glycoside hydrolysis and (+)-catechin transglycosylation
复制标题
来自 Novosphingobium sp GX9 的 β-葡萄糖苷酶，对异黄酮糖苷水解和 ( )-儿茶素转糖基化具有高催化效率
DOI：
10.1007/s00253-014-5661-3
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发表时间：
2014-08-01
影响因子：
5
通讯作者：
Huang, Ribo
中科院分区：
文献类型：
--
作者：
Du, Liqin;Wang, Zilong;Huang, Ribo
鉴于β-内酰胺酶及其相关糖缀合物在人类健康中的重要作用，对其酶促转化有相当大的兴趣。SBGL是从新鞘氨醇菌GX 9中分离得到的一种新型β-葡萄糖苷酶，在大肠杆菌中得到表达，并发现其对大豆苷和染料木苷具有较高的水解活性。SBGL显示大豆苷和染料木苷的K（m）值非常低，这些底物的k（cat）/K（m）值分别为33，300和19，200 s（-1）mM（-1）。SBGL葡糖苷酶还可以在饱和受体浓度下将黄烷醇（+）-儿茶素转糖基化，这对于β-葡糖苷酶先前没有报道并且难以合成实现。
In view of the important role of isoflavonoids and their related glycoconjugates in human health, there is considerable interest in their enzymatic conversion. SBGL, a novel beta-glucosidase isolated from Novosphingobium sp. GX9, was expressed in Escherichia coli and found to have high activity for hydrolysis of daidzin and genistin. SBGL showed very low K (m) values for daidzin and genistin, and the k (cat)/K (m) values for these substrates were 33,300 and 19,200 s(-1) mM(-1), respectively. The SBGL glucosidase could also transglycosylate the flavanol (+)-catechin at saturating acceptor concentrations, which has not previously been reported for a beta-glucosidase and is difficult to achieve synthetically.