Abstract:
: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 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Day AJ,Cañada FJ,Díaz JC,Kroon PA,Mclauchlan R,Faulds CB,Plumb GW,Morgan MR,Williamson Gdoi
10.1016/s0014-5793(00)01211-4keywords:
subject
Has Abstractpub_date
2000-02-25 00:00:00pages
166-70issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01211-4journal_volume
468pub_type
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