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Possible Evidence of Contamination by Catechins in Deconjugation Enzymes From Helix Pomatia and Abalone Entrails

Possible Evidence of Contamination by Catechins in Deconjugation Enzymes From Helix Pomatia and Abalone Entrails

Toshiyuki Nakamura, Ryohei Tanaka, Hitoshi Ashida

Biosci Biotechnol Biochem. 2011;75(8):1506-10.

PMID: 21821947

Abstract:

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 β-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 β-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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR424866	β-Glucuronidase from abalone			Price

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