Purification and Properties of a Glucuronan Lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472)-Reference-Cited by-同舟云学术

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

Published:2001-11 Issue:11 Volume:67 Page:5197-5203
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Da Costa Alexandre¹,Michaud Philippe¹,Petit Emmanuel¹,Heyraud Alain²,Colin-Morel Philippe²,Courtois Bernard¹,Courtois Josiane¹

Affiliation:

1. 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

2. CERMAV-CNRS Université Joseph Fourrier, 38041 Grenoble Cedex,2 France

Abstract

ABSTRACT 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. Zn 2+ , Cu 2+ , and Hg 2+ (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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/AEM.67.11.5197-5203.2001

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