Purification and characterization of microbial gellan lyase.
AUTOR(ES)
Hashimoto, W
RESUMO
Gellan lyase was purified from the culture fluid of soil samples incubated in a medium containing gellan as a sole carbon source. The enzyme was a monomer with a molecular mass of 140 kDa and was most active at pH 7.5 and 45 degrees C. The enzyme was highly specific to gellan and lowered the viscosity of the polymer.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=167921Documentos Relacionados
- Purification and characterization of Acinetobacter calcoaceticus isocitrate lyase.
- Microbial distribution of selenocysteine lyase.
- Purification and properties of streptococcal hyaluronate lyase.
- Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase.
- p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase.
