Dietary flavonoid and isoflavone glycosides are hydrolysed by the lactase site of lactase phlorizin hydrolase
Dietary flavonoid and isoflavone glycosides are hydrolysed by the lactase site of lactase phlorizin hydrolase
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DOI：
10.1016/s0014-5793(00)01211-4
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发表时间：
2000-02-25
期刊：
影响因子：
3.5
通讯作者：
Williamson, G
中科院分区：
文献类型：
--
作者：
Day, AJ;Cañada, FJ;Williamson, G
乳糖酶根茎苷水解酶(LPH；EC 3.2.1.62)是发现于哺乳动物小肠刷状缘的一种膜结合型β-糖苷酶，从绵羊小肠中提纯出来的LPH能水解黄酮醇和异黄酮苷。酶的催化效率(k(CAT)/K-m)分别为170、137、77和11(mm~(-1))S，酶活性主要集中在乳糖酶，而不是根皮苷。LPH对膳食(Iso)黄酮苷的脱糖能力表明这种酶可能在这些生物活性化合物的新陈代谢中发挥作用。(C)2000年欧洲生化学会联合会。
Lactase phlorizin hydrolase (LPH; EC 3.2.1.62) is a membrane-bound, family 1 beta-glycosidase found on the brush border of the mammalian small intestine, LPH purified from sheep small intestine, was capable of hydrolysing a range of flavonol and isoflavone glycosides. The catalytic efficiency (k(cat)/ K-m) for the hydrolysis of quercetin-4'-glucoside, quercetin-3-glucoside, genistein-7-glucoside and daidzein-7-glucoside was 170, 137, 77 and 1 1 (mM(-1) s(-1)) respectively, The majority of the activity occurred at the lactase and not phlorizin hydrolase site. The ability of LPH to deglycosylate dietary (iso)flavonoid glycosides suggests a possible role for this enzyme in the metabolism of these biologically active compounds. (C) 2000 Federation of European Biochemical Societies.