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

AUTOR(ES)

Da Costa, Alexandre

FONTE

American Society for Microbiology

RESUMO

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.

Documentos Relacionados

• Adsorption of Rhodococcus Strain GIN-1 (NCIMB 40340) on Titanium Dioxide and Coal Fly Ash Particles
• Partial Purification and Some Properties of Tyrosine Phenol-Lyase from Aeromonas phenologenes ATCC 29063 1
• Molecular Cloning, Purification, and Biochemical Characterization of Hydantoin Racemase from the Legume Symbiont Sinorhizobium meliloti CECT 4114
• Purification and properties of streptococcal hyaluronate lyase.
• Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties.