lignans and flavan-3-ol

lignans has been researched along with flavan-3-ol* in 1 studies

Other Studies

1 other study(ies) available for lignans and flavan-3-ol

Article	Year
Isolation and characterization of a human intestinal bacterium Eggerthella sp. CAT-1 capable of cleaving the C-ring of (+)-catechin and (-)-epicatechin, followed by p-dehydroxylation of the B-ring. Biological & pharmaceutical bulletin, 2012, Volume: 35, Issue:12 We isolated a human intestinal bacterium, capable of cleaving the C-ring and dehydroxylating the B-ring of both (+)-catechin (2R,3S) and (-)-epicatechin (2R,3R). Although the strain was classified as Eggerthella (Eg.) lenta [named Eg. sp. CAT-1 (JF798636)] by 16S ribosomal RNA (rRNA) gene similarity, it was quite different in substrate specificity from a previously isolated strain, Eg. sp. SDG-2, which takes part in cleavage of the C-ring and dehydroxylation of the 3,4-dihydroxyphenyl moiety (B-ring) of (3R)-flavan-3-ol derivatives. On the other hand, both Eg. sp. CAT-1 and Eg. sp. SDG-2 showed the same substrate specificity against dehydroxylation of enantiomeric lignans, (+)- and (-)-dihydroxyenterodiol, and (+)- and (-)-dihydroxyenterolactone. Topics: Actinobacteria; Catechin; Flavonoids; Genes, Bacterial; Humans; Hydroxylation; Intestinal Mucosa; Intestines; Lignans; RNA, Ribosomal, 16S; Species Specificity	2012

Article

Year

Isolation and characterization of a human intestinal bacterium Eggerthella sp. CAT-1 capable of cleaving the C-ring of (+)-catechin and (-)-epicatechin, followed by p-dehydroxylation of the B-ring.

Biological & pharmaceutical bulletin, 2012, Volume: 35, Issue:12

We isolated a human intestinal bacterium, capable of cleaving the C-ring and dehydroxylating the B-ring of both (+)-catechin (2R,3S) and (-)-epicatechin (2R,3R). Although the strain was classified as Eggerthella (Eg.) lenta [named Eg. sp. CAT-1 (JF798636)] by 16S ribosomal RNA (rRNA) gene similarity, it was quite different in substrate specificity from a previously isolated strain, Eg. sp. SDG-2, which takes part in cleavage of the C-ring and dehydroxylation of the 3,4-dihydroxyphenyl moiety (B-ring) of (3R)-flavan-3-ol derivatives. On the other hand, both Eg. sp. CAT-1 and Eg. sp. SDG-2 showed the same substrate specificity against dehydroxylation of enantiomeric lignans, (+)- and (-)-dihydroxyenterodiol, and (+)- and (-)-dihydroxyenterolactone.

Topics: Actinobacteria; Catechin; Flavonoids; Genes, Bacterial; Humans; Hydroxylation; Intestinal Mucosa; Intestines; Lignans; RNA, Ribosomal, 16S; Species Specificity

2012