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First bacterial chalcone isomerase isolated from Eubacterium ramulus.

Claudia Herles1, Annett Braune, Michael Blaut

  • 1Abteilung Gastrointestinale Mikrobiologie, Deutsches Institut für Ernährungsforschung Potsdam-Rehbrücke, Arthur-Scheunert-Allee 114-116, 14558, Nuthetal, Germany.

Archives of Microbiology
|May 6, 2004
PubMed
Summary

Eubacterium ramulus possesses a novel bacterial chalcone isomerase enzyme. This enzyme converts flavanones like naringenin into chalcones, a key step in flavonoid degradation.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Enzymology

Background:

  • Eubacterium ramulus, a human gut anaerobe, degrades various flavonoids.
  • Flavonoid degradation pathways often begin with isomerization of flavanones to chalcones.

Purpose of the Study:

  • To identify and characterize a chalcone isomerase from Eubacterium ramulus.
  • To investigate the enzyme's role in naringenin metabolism.

Main Methods:

  • Purification of chalcone isomerase from E. ramulus cell-free extracts.
  • Enzyme activity assays using various chalcone substrates.
  • Determination of enzyme molecular mass and subunit composition.

Main Results:

  • A bacterial chalcone isomerase was purified to homogeneity.

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  • The enzyme exhibited activity on naringenin chalcone, isoliquiritigenin, and butein.
  • Molecular mass was estimated at 136/129 kDa (native) with a 30 kDa subunit.
  • N-bromosuccinimide, naringenin, and phloretin inhibited the enzyme.
  • Conclusions:

    • This is the first report of a bacterial chalcone isomerase.
    • The enzyme likely plays a role in the conversion of naringenin to its chalcone form.
    • Further research is needed to elucidate its precise physiological function.