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Applied and Environmental Microbiology, December 1998, p. 4743-4747, Vol. 64, No. 12
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Purification and Characterization of Gallic Acid Decarboxylase from Pantoea agglomerans T71

Mitsuhiro Zeida,1 Marco Wieser,2 Toyokazu Yoshida,2 Tsuyoshi Sugio,1 and Toru Nagasawa2,*

Department of Biological Function & Genetic Resources Sciences, Faculty of Agriculture, Okayama University, Tsushima Naka, Okayama 700-11,1 and Department of Biomolecular Science, Faculty of Engineering, Gifu University, Gifu-Yanagido 501-11,2 Japan

Received 27 May 1998/Accepted 6 September 1998

Oxygen-sensitive gallic acid decarboxylase from Pantoea (formerly Enterobacter) agglomerans T71 was purified from a cell extract after stabilization by reducing agents. This enzyme has a molecular mass of approximately 320 kDa and consists of six identical subunits. It is highly specific for gallic acid. Gallic acid decarboxylase is unique among similar decarboxylases in that it requires iron as a cofactor, as shown by plasma emission spectroscopy (which revealed an iron content of 0.8 mol per mol of enzyme subunit), spectrophotometric analysis (absorption shoulders at 398 and 472 nm), and inhibition of the enzyme activity by 2,2'-bipyridyl, o-phenanthroline, and EDTA. Another interesting feature of this strain is the fact that it contains a tannase, which is used together with the gallic acid decarboxylase in a two-enzyme resting cell bioconversion to synthesize valuable pyrogallol from readily available tannic acid.

* Corresponding author. Mailing address: Department of Biomolecular Sciences, Faculty of Engineering, Gifu University, Gifu-Yanagido, Japan 501-11. Phone and fax: (81)-58-293-2647. E-mail: tonagasa{at}apchem.gifu-u.ac.jp.

Applied and Environmental Microbiology, December 1998, p. 4743-4747, Vol. 64, No. 12
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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