Previous Article | Next Article ![]()
Applied and Environmental Microbiology, November 2001, p. 5197-5203, Vol. 67, No. 11
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.
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)
*
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.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»