Purification and some properties of Pseudomonas fluorescens lipase.
Lipase (triacylglycerol lipase, EC 3.1.1.3) has been purified from Pseudomonas fluorescens wild strain by chromatography on DEAE-cellulose and octyl-Sepharose CL-4B. The yield was 21% and the specific activity of the purified enzyme 4780 U/mg protein. It showed a Mr of about 45 x 10(4) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is active over a wide pH range and at 50-55 degrees C.
Sztajer
H
H
Institute of Organic and Physical Chemistry, Technical University of Wroclaw, Poland.
Borkowski
J
J
Sobiech
K
K
D011232:Chemical Precipitation; D002847:Chromatography, Agarose; D002848:Chromatography, DEAE-Cellulose; D004589:Electrophoresis, Disc; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000302:isolation & purification* / Q000378:metabolism; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D012685:Sepharose / Q000031:analogs & derivatives; D013696:Temperature
C027176:octyl-sepharose CL-4B; D012685:Sepharose; D008049:Lipase