Purification and properties of a glucuronan lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472)

被引：24

作者：

Da Costa, A

Michaud, P

Petit, E

Heyraud, A

Colin-Morel, P

Courtois, B

Courtois, J

机构：

[1] Univ Picardie, Dept Genie Biol, IUT, Lab Polysaccharides Microbiens & Vegetaux, F-80025 Amiens, France

[2] Univ Grenoble 1, CNRS, CERMAV, F-38041 Grenoble, France

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2001年 / 67卷 / 11期

关键词：

D O I：

10.1128/AEM.67.11.5197-5203.2001

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 [微生物学]; 0836 [生物工程]; 090102 [作物遗传育种]; 100705 [微生物与生化药学];

摘要：

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 pl 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 degreesC. 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.

引用

页码：5197 / 5203

页数：7

共 45 条

[1]

ALTMAN E, 1986, S AFR J SCI, V82, P45

[2]

BERINGER JE, 1974, J GEN MICROBIOL, V84, P188

[3]

L-GULURONAN-SPECIFIC ALGINATE LYASE FROM A MARINE BACTERIUM ASSOCIATED WITH SARGASSUM [J].