Purification and partial characterization of an alkaline lipase from Pseudomonas pseudoalcaligenes F-111.
AUTOR(ES)
Lin, S F
RESUMO
An extracellular alkaline lipase of alkalophilic Pseudomonas pseudoalcaligenes F-111 was purified to homogeneity. The apparent molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was 32,000, and the isoelectric point was 7.3. With p-nitrophenyl esters as its substrates, the enzyme shows preference for C12 acyl and C14 acyl groups. It was stable in the pH range of 6 to 10, which coincides with the optimum pH range.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=167873Documentos Relacionados
- Purification and Characterization of Maleate Hydratase from Pseudomonas pseudoalcaligenes
- Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45.
- A Cold-Adapted Lipase of an Alaskan Psychrotroph, Pseudomonas sp. Strain B11-1: Gene Cloning and Enzyme Purification and Characterization
- Partial purification and characterization of thiosulfate oxidase from Pseudomonas aeruginosa.
- Purification, Characterization, and Sequence Analysis of 2-Aminomuconic 6-Semialdehyde Dehydrogenase from Pseudomonas pseudoalcaligenes JS45
