Dietary flavonoid and isoflavone glycosides are hydrolysed by the lactase site of lactase phlorizin hydrolase

FEBS Letters - Tập 468 - Trang 166-170 - 2000
Andrea J Day1, F.Javier Cañada2, Juan C Dı́az2, Paul A Kroon1, Russell Mclauchlan1, Craig B Faulds1, Geoff W Plumb1, Michael R.A Morgan3, Gary Williamson1
1Diet, Health and Consumer Science Division, Institute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, UK
2Instituto de Quı́mica Orgánica, Consejo Superior de Investigaciones Cientı́ficas, Juan de la Cierva 3, 28006 Madrid, Spain
3Proctor Department of Food Science, University of Leeds, Leeds LS2 9JT, UK

Tóm tắt

Lactase phlorizin hydrolase (LPH; EC 3.2.1.62) is a membrane‐bound, family 1 β‐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 14 (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.

Tài liệu tham khảo

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FEBS Letters

Tập 468

166-170

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