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Vol. 15, No. 1-4, 2005
Issue release date: 2005
Section title: Original Paper
Cell Physiol Biochem 2005;15:089–098

Enzymatic Oxidation of Vanillin, Isovanillin and Protocatechuic Aldehyde with Freshly Prepared Guinea Pig Liver Slices

Panoutsopoulos G.I.1,2 · Beedham C.1
1Department of Pharmaceutical Chemistry, School of Pharmacy, University of Bradford, 2School of Biochemistry and Biotechnology, University of Thessaly
email Corresponding Author

Dr Georgios I. Panoutsopoulos

5 Tenedou Street, Platia Amerikis, Athens 112 57 (Greece)

Université de Lausanne, CH–1005 Lausanne (Switzerland)

Tel. +30210-8649617, Fax: +30210-8649617


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Background/Aims: The oxidation of xenobiotic-derived aromatic aldehydes with freshly prepared liver slices has not been previously reported. The present investigation compares the relative contribution of aldehyde oxidase, xanthine oxidase and aldehyde dehydrogenase activities in the oxidation of vanillin, isovanillin and protocatechuic aldehyde with freshly prepared liver slices. Methods: Vanillin, isovanillin or protocatechuic aldehyde was incubated with liver slices in the presence/absence of specific inhibitors of each enzyme, followed by HPLC. Results: Vanillin was rapidly converted to vanillic acid. Vanillic acid formation was completely inhibited by isovanillin (aldehyde oxidase inhibitor), whereas disulfiram (aldehyde dehydrogenase inhibitor) inhibited acid formation by 16% and allopurinol (xanthine oxidase inhibitor) had no effect. Isovanillin was rapidly converted to isovanillic acid. The formation of isovanillic acid was not altered by allopurinol, but considerably inhibited by disulfiram. Protocatechuic aldehyde was converted to protocatechuic acid at a lower rate than that of vanillin or isovanillin. Allopurinol only slightly inhibited protocatechuic aldehyde oxidation, isovanillin had little effect, whereas disulfiram inhibited protocatechuic acid formation by 50%. Conclusions: In freshly prepared liver slices, vanillin is rapidly oxidized by aldehyde oxidase with little contribution from xanthine oxidase or aldehyde dehydrogenase. Isovanillin is not a substrate for aldehyde oxidase and therefore it is metabolized to isovanillic acid predominantly by aldehyde dehydrogenase. All three enzymes contribute to the oxidation of protocatechuic aldehyde to its acid.

© 2005 S. Karger AG, Basel

Article / Publication Details

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Abstract of Original Paper

Accepted: 9/14/2004
Published online: 1/13/2005
Issue release date: 2005

Number of Print Pages: 10
Number of Figures: 0
Number of Tables: 0

ISSN: 1015-8987 (Print)
eISSN: 1421-9778 (Online)

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