Possible evidence of contamination by catechins in deconjugation enzymes from Helix pomatia and Abalone entrails

Toshiyuki Nakamura, Ryohei Tanaka, Hitoshi Ashida

Research output: Contribution to journalArticle

5 Citations (Scopus)


β-Glucuronidase and sulfatase are the major deconjugating enzymes used in the cleavage of the glucuronate and sulfate moieties, respectively, from certain conjugated food factors including polyphenols. In the present study, we found that compounds having the same molecular weights as catechins were present in Helix pomatia- and/or Abalone entrails-derived μ-glucuronidase and sulfatase by liquid chromatography tandem mass spectrometry (LC-MS/MS) with multiple reaction monitoring methods. On the other hand, the same molecular weights as catechins were undetectable in Escherichia coli-derived μ-glucuronidase and Aerobacter aerogenes-derived sulfatase. By high performance liquid chromatography, enzyme-derived catechins were not detected because of approximately 1,000-fold lower sensitivity as compared to LC-MS/MS. These results suggest that the catechins in these enzymes might be attributed to the diets of the organisms as the enzyme sources.

Original languageEnglish
Pages (from-to)1506-1510
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Issue number8
Publication statusPublished - 2011
Externally publishedYes



  • β-glucuronidase
  • Catechin
  • Liquid chromatography tandem mass spectrometry (LC-MS/MS)
  • Sulfatase

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Analytical Chemistry
  • Organic Chemistry

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