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