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Dietary flavonoid and isoflavone glycosides are hydrolysed by the lactase site of lactase phlorizin hydrolase
Author(s) -
Day Andrea J,
Cañada F.Javier,
Dı́az Juan C,
Kroon Paul A,
Mclauchlan Russell,
Faulds Craig B,
Plumb Geoff W,
Morgan Michael R.A,
Williamson Gary
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01211-4
Subject(s) - lactase , biochemistry , glycoside hydrolase , chemistry , glucoside , glycoside , hydrolase , flavonoid , phlorizin , genistein , quercetin , hydrolysis , beta glucosidase , aglycone , enzyme , enzyme assay , biology , stereochemistry , glucose transporter , endocrinology , medicine , alternative medicine , antioxidant , pathology , insulin
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.