Metabolism of rutin and poncirin by human intestinal microbiota and cloning of their metabolizing α-L-rhamnosidase from Bifidobacterium dentium.

@article{Bang2015MetabolismOR,
  title={Metabolism of rutin and poncirin by human intestinal microbiota and cloning of their metabolizing $\alpha$-L-rhamnosidase from Bifidobacterium dentium.},
  author={Seo-Hyeon Bang and Yang-Jin Hyun and Ju-Sun Shim and Sung-Woon Hong and Dong-Hyun Kim},
  journal={Journal of microbiology and biotechnology},
  year={2015},
  volume={25 1},
  pages={
          18-25
        }
}
To understand the metabolism of flavonoid rhamnoglycosides by human intestinal microbiota, we measured the metabolic activity of rutin and poncirin (distributed in many functional foods and herbal medicine) by 100 human stool specimens. The average α-Lrhamnosidase activities on the p-nitrophenyl-α-L-rhamnopyranoside, rutin, and poncirin subtrates were 0.10 ± 0.07, 0.25 ± 0.08, and 0.15 ± 0.09 pmol/min/mg, respectively. To investigate the enzymatic properties, α-L-rhamnosidase-producing bacteria… 

Figures and Tables from this paper

Purification and Characterization of a Novel α-L-Rhamnosidase from Papiliotrema laurentii ZJU-L07 and Its Application in Production of Icariin from Epimedin C

The enzymatic hydrolysis method could be used for the industrialized production of icariin and could also cleave the α-1,2 glycosidic linkage between glucoside and rhamnoside in naringin and neohesperidin, which could be applicable in other biotechnological processes.

Production of a Recombinant α-l-Rhamnosidase from Aspergillus niger CCTCC M 2018240 in Pichia pastoris

This process offers a simple and effective approach for the large-scale production of α-l-rhamnosidase through high density-induced fermentation based on a glycerol feeding strategy in a 3-L bioreactor.

Conversion of Rutin, a Prevalent Dietary Flavonol, by the Human Gut Microbiota

A fluorescence-based single-cell activity measure [biorthogonal non-canonical ammino acid-tagging (BONCAT)] combined with fluorescence activated cell sorting (FACS) was used to determine which microorganisms are metabolically-active after amendment of the flavonoid rutin to suggest individual microbiotas differ in their ability to metabolize r Rutin and utilize different conversion pathways.

Rhamnosidase activity of selected probiotics and their ability to hydrolyse flavonoid rhamnoglucosides

Rhamnosidases from the tested probiotics are substrate specific cleaving hesperidin, narcissin and to a small extent rutin, but not naringin, indicating that narcissin acts as an inducer.

A comprehensive study of the metabolism of flavonoid oroxin B in vivo and in vitro by UHPLC-Q-TOF-MS/MS.

Degradation Kinetics of 6‴-p-Coumaroylspinosin and Identification of Its Metabolites by Rat Intestinal Flora.

A high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) method was developed to determine P-CS for investigating the degradation characteristics of P- CS incubated with rat feces and showed that P-cs degraded rapidly and the degradation speeds varied depending upon theP-CS concentrations.

Characterization of a glycoside hydrolase family 78 α-l-rhamnosidase from Bacteroides thetaiotaomicron VPI-5482 and identification of functional residues

Recombinant BtRha78A exhibited a good pH stability and relatively high thermostability and could be tolerant of a low concentration of alcohols, which made it a promising alternative biocatalyst for industrial applications.

Computational study of the main flavonoids from Chrysobalanus icaco L. against NADPH-oxidase and in vitro Antioxidant Activity

The results demonstrate for the first time the in silico action of quercetin against NOX, as well as reiterate the antioxidant potential of C. icaco.
...

References

SHOWING 1-10 OF 32 REFERENCES

Characterization of Two Distinct Glycosyl Hydrolase Family 78 α-l-Rhamnosidases from Pediococcus acidilactici

Detailed kinetic data is presented on two novel rhamnosidases from Pediococcus acidilactici DSM 20284, probably representing two subclasses within GH 78, which could be relevant for the further study of bacterial glycosidases.

Inhibitory effects ofBifidobacterium Spp. isolated from a healthy korean on harmful enzymes of human intestinal microflora

Five hundreds of bifidobacteria were isolated from a healthy Korean and the inhibitory effects of these isloated bacteria on harmful enzymes of human intestinal microflora were examined by

Purification and Characterization of an α-L-Rhamnosidase from Pichia angusta X349

  • T. YanaiM. Sato
  • Chemistry, Biology
    Bioscience, biotechnology, and biochemistry
  • 2000
An intracellular α-L-rhamnosidase from Pichia angusta X349 was purified to homogeneity through four chromatographic steps. The α-L-rhamnosidase appeared to be a monomeric protein with a molecular

Physiological and biochemical characterization of the two alpha-L-rhamnosidases of Lactobacillus plantarum NCC245.

This work identified and characterized the strain L. plantarum NCC245 and its two alpha-l-rhamnosidase enzymes, which might be applied for improvement of bioavailability of health-beneficial polyphenols, such as hesperidin, in humans.

Characterization of Rhamnosidases from Lactobacillus plantarum and Lactobacillus acidophilus

Rhamnose removal was confirmed, indicating that rhamnosidase-producing bacteria may find commercial application, depending on the technological properties of the strains and enzymes.

Purification and characterization of alpha-L-rhamnosidase from Bacteroides JY-6, a human intestinal bacterium.

  • I. JangD. Kim
  • Chemistry, Biology
    Biological & pharmaceutical bulletin
  • 1996
An alpha-L- rhamnosidase was purified 1500-fold from Bacteroides JY-6, an intestinal anaerobic bacterium of human and was strongly inhibited by L-rhamnose, L-fucose, saccharic acid 1,4-lactone, p-chlormercuriphenylsulfonic acid and Pb2+.

Anti-Helicobacter pylori activity of the metabolites of poncirin from Poncirus trifoliata by human intestinal bacteria.

Poncirin was isolated from water extract of the fruits of Poncirus trifoliata and metabolized by human intestinal bacteria and its metabolites except ponciretin did not inhibit the growth of HP, nor did they inhibit HP urease.

Purification and characterization of an alpha-L-rhamnosidase from Aspergillus nidulans.

An enzyme exhibiting alpha-L-rhamnosidase activity was purified by fractionating a culture filtrate of Aspergillus nidulans grown on L- rhamnose as the sole carbon source, showing the enzyme to be N-glycosylated and active both on alpha-1,2 and alpha- 1,6 linkages to beta-D-glucosides.

Purification and characterization of intracellular α-l-rhamnosidase from Pseudomonas paucimobilis FP2001

Examination of the substrate specificity using various synthetic and natural l-rhamnosyl glycosides showed that this enzyme had a relatively broader substrate specificity than those reported so far.

The thermostable α‐l‐rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial α‐l‐rhamnoside hydrolase, a new type of inverting glycoside hydrolase

An α‐l‐rhamnosidase clone was isolated from a genomic library of the thermophilic anaerobic bacterium Clostridium stercorarium and its primary structure was determined, indicating a single displacement mechanism.