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Applied and Environmental Microbiology, November 2001, p. 5197-5203, Vol. 67, No. 11
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.11.5197-5203.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Purification and Properties of a Glucuronan Lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472)

Alexandre Da Costa,1 Philippe Michaud,1 Emmanuel Petit,1 Alain Heyraud,2 Philippe Colin-Morel,2 Bernard Courtois,1 and Josiane Courtois1,*

Laboratoire des Polysaccharides Microbiens et Végétaux, IUT, Département de Génie Biologique, Université de Picardie Jules Verne, Avenue des Facultés, Le Bailly, 80025 Amiens Cedex,1 and CERMAV-CNRS Université Joseph Fourrier, 38041 Grenoble Cedex,2 France

Received 10 April 2001/Accepted 4 September 2001

A glucuronan lyase extracted from Sinorhizobium meliloti strain M5N1CS was purified to homogeneity by anion-exchange chromatography. The purified enzyme corresponds to a monomer with a molecular mass of 20 kDa and a pI of 4.9. A specific activity was found only for polyglucuronates leading to the production of 4,5-unsaturated oligoglucuronates. The enzyme activity was optimal at pH 6.5 and 50°C. Zn2+, Cu2+, and Hg2+ (1 mM) inhibited the enzyme activity. No homology of the enzyme N-terminal amino acid sequence was found with any of the previously published protein sequences. This enzyme purified from S. meliloti strain M5N1CS corresponding to a new lyase was classified as an endopolyglucuronate lyase.


* Corresponding author. Mailing address: Laboratoire des Polysaccharides Microbiens et Végétaux, IUT, Département de Génie Biologique, Avenue des Facultés, Le Bailly, 80025 Amiens, France. Phone: (33) (3) 22 53 40 99. Fax: (33) (3) 22 95 62 54. E-mail: Josiane.Courtois{at}iut.u-picardie.fr.


Applied and Environmental Microbiology, November 2001, p. 5197-5203, Vol. 67, No. 11
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.11.5197-5203.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



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