title: Purification and partial characterization of an alkaline lipase from Pseudomonas pseudoalcaligenes F-111.
abstract: 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.
authors.affiliation: Department of Bioengineering, Tatung Institute of Technology, Taipei, Taiwan, Republic of China.
authors.forename: S F
authors.initials: SF
authors.lastname: Lin
authors.forename: C M
authors.initials: CM
authors.lastname: Chiou
authors.forename: C M
authors.initials: CM
authors.lastname: Yeh
authors.forename: Y C
authors.initials: YC
authors.lastname: Tsai
mesh_terms: D000595:Amino Acid Sequence; D008049:Lipase / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D008049:Lipase