Properties and applications of β‐glycosidase from <i>Bacteroides thetaiotaomicron</i> that specifically hydrolyses isoflavone glycosides

Byun, Dahye; Choi, Ho‐Young; Lee, Hye Won; Jeon, Hye-Yeon; Choung, Woo-Jae; Shim, Jae‐Hoon

doi:10.1111/ijfs.12786

Cited by 9 publications

(11 citation statements)

References 32 publications

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“…A second class of O -glycosidases was observed in Catenibacillus scindens , where a cluster of two genes, dfgCD, was characterized to encode an enzyme that 7- O -deglycosylated isoflavones and flavones [ 17 ]. DfgCD homologs are found scarcely in human gut MAGs, mainly in Hungatella hathewayi , Faecalicatena species, and Eisenbergiella sp900066775, all with approximately 100 occurrences ( Supplementary Figure S3 ).…”

Section: Resultsmentioning

confidence: 99%

“…The current gene clusters reported to play a role in C-deglycosylation are depicted Figure 3. Of the Eubacterium cellulosolvens dfgABCDE gene cluster (Figure 3A, [17]), all 1; hits with a lower PID are shown in Supplementary Figure S4). Hits were filtered for at least 20 occurrences, so that each bubble represents a number of redundant sequences ranging from 20 to 2176.…”

Section: C-deglycosylation Of Flavonoidsmentioning

confidence: 99%

“…Of the dgp gene cluster of strain PUE (Figure 3B), we used only the first three genes (dgpABC) as queries, since only these genes were shown to catalyze reactions in the C-deglycosylation pathway [25,26]. [17] and (B) strain PUE [25,26], with dgpA encoding an oxidoreductase and dgpBC as oxo-puerarin-deglycosylating enzymes, of which all three are involved in C-deglycosylation. Genes encoding deglycosylating enzymes are shown in turquoise, accessory genes in violet.…”

Section: C-deglycosylation Of Flavonoidsmentioning

confidence: 99%

“…Many described gut bacterial flavonoid-converting activities lack biochemical or genetic analyses and, therefore, sequences of the involved enzymes. Of the O -deglycosylating enzymes, six beta-galactosidases [ 15 , 16 , 17 ] and a set of flavonoid-active rhamnosidases [ 18 ] that cleave the terminal rhamnose subunit of flavonoid rhamnosides (e.g., rutin or naringin), resulting in the corresponding flavonoid glucosides [ 19 , 20 , 21 , 22 , 23 , 24 ], have been characterized ( Table 1 ). The more complex C -deglycosylating enzyme systems were studied in fewer gut bacteria [ 25 , 26 , 27 ] ( Table 1 ).…”

Section: Introductionmentioning

confidence: 99%

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Flavonoid-Modifying Capabilities of the Human Gut Microbiome—An In Silico Study

2021

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Flavonoids are a major group of dietary plant polyphenols and have a positive health impact, but their modification and degradation in the human gut is still widely unknown. Due to the rise of metagenome data of the human gut microbiome and the assembly of hundreds of thousands of bacterial metagenome-assembled genomes (MAGs), large-scale screening for potential flavonoid-modifying enzymes of human gut bacteria is now feasible. With sequences of characterized flavonoid-transforming enzymes as queries, the Unified Human Gastrointestinal Protein catalog was analyzed and genes encoding putative flavonoid-modifying enzymes were quantified. The results revealed that flavonoid-modifying enzymes are often encoded in gut bacteria hitherto not considered to modify flavonoids. The enzymes for the physiologically important daidzein-to-equol conversion, well studied in Slackiaisoflavoniconvertens, were encoded only to a minor extent in Slackia MAGs, but were more abundant in Adlercreutzia equolifaciens and an uncharacterized Eggerthellaceae species. In addition, enzymes with a sequence identity of about 35% were encoded in highly abundant MAGs of uncultivated Collinsella species, which suggests a hitherto uncharacterized daidzein-to-equol potential in these bacteria. Of all potential flavonoid modification steps, O-deglycosylation (including derhamnosylation) was by far the most abundant in this analysis. In contrast, enzymes putatively involved in C-deglycosylation were detected less often in human gut bacteria and mainly found in Agathobacter faecis (formerly Roseburia faecis). Homologs to phloretin hydrolase, flavanonol/flavanone-cleaving reductase and flavone reductase were of intermediate abundance (several hundred MAGs) and mainly prevalent in Flavonifractor plautii. This first comprehensive insight into the black box of flavonoid modification in the human gut highlights many hitherto overlooked and uncultured bacterial genera and species as potential key organisms in flavonoid modification. This could lead to a significant contribution to future biochemical-microbiological investigations on gut bacterial flavonoid transformation. In addition, our results are important for individual nutritional recommendations and for biotechnological applications that rely on novel enzymes catalyzing potentially useful flavonoid modification reactions.

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Section: Resultsmentioning

confidence: 99%

Section: C-deglycosylation Of Flavonoidsmentioning

confidence: 99%

Section: C-deglycosylation Of Flavonoidsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Flavonoid-Modifying Capabilities of the Human Gut Microbiome—An In Silico Study

2021

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“…pseudocatenulatum and Bacteroides thetaiotaomicron. [14,15,35]. Several avonols and iso avones (e.g.…”

Section: Introductionmentioning

confidence: 99%

Flavonoid-modifying capabilities of the gut microbiome – an in silico study

Goris

Cuadrat

Braune

2021

Preprint

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Flavonoids are a major group of dietary plant polyphenols and have a positive health impact, but their modification and degradation in the human gut is still widely unknown. Due to the rise of human gut metagenome data and the assembly of hundreds of thousands of bacterial metagenome-assembled genomes (MAGs), large-scale screening for potential flavonoid-modifying enzymes is now feasible. With sequences from characterized flavonoid-transforming enzymes as queries, the Unified Human Gastrointestinal Protein catalog was analyzed and quantification of putative flavonoid-modifying enzymes was carried out. The results revealed that flavonoid-modifying enzymes are often highly abundant in bacteria hitherto not considered as flavonoid-modifying gut bacteria. The enzymes for the physiologically important daidzein to equol conversion, well studied in Slackia isoflavoniconvertens, were encoded only to a low extent in Slackia MAGs, but more abundant in Adlercreutzia equolifaciens and an uncharacterizedEggerthellaceae species. In addition, a high abundance of genes with a similarity of only about 35% in uncultivated Collinsella species suggest a hitherto uncharacterized Daidzein-to-equol potential in these bacteria. Of all potential flavonoid modification steps, O-deglycosylation (including derhamnosylation) was by far the most abundant in this analysis. In contrast, enzymes putatively involved in C-deglycosylation were detected less often in human gut bacteria and mainly found in Agathobacter faecis (formerly Roseburia faecis). Phloretin hydrolase, flavanonol/flavanone-cleaving reductase and flavone reductase (all three most abundant in Flavonifractor plautii) and O-demethylase (Intestinibacter bartlettii) homologs were of intermediate prevalence (several hundreds of MAGs). This first comprehensive insight into the black box of flavonoid modification in the human gut highlights many hitherto overlooked and uncultured bacterial genera and species as key organisms in flavonoid modification by the human gut microbiota. This could lead to a significant contribution to future biochemical-microbiological investigations on gut bacterial flavonoid transformation. In addition, our results are important for individual nutritional recommendations and for biotechnological applications which rely on novel enzymes catalyzing potentially useful flavonoid modification reactions.

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