Purification and some properties of Pseudomonas fluorescens lipase
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H Sztajer1, J Borkowski, K Sobiech
1Institute of Organic and Physical Chemistry, Technical University of Wroclaw, Poland.
Biotechnology and Applied Biochemistry
|February 1, 1991
Abstract:
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.