Purification and some characteristics of Penicillium citrinum lipase
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An extracellular lipase (glycerol ester hydrolases E.C. 188.8.131.52.) was isolated from a culture filtrate of Penicillium citrinum. The purification procedure included ammonium sulfate precipitation, ultrafiltration and chromatography on Octyl-Sepharose CL-4B. The enzyme was 400-fold purified with 9.66% yield. The molecular weight has been estimated by polyacrylamide gel electrophoresis under denaturing conditions at 26000. On the other hand, lipase forms active dimers and tetramers aggregates as observed after native PAGE. Lipase from Penicillium citrinum showed a preference for triacylglycerols. It is non-specific and hydrolyzes each of the three ester bonds of triacylglycerols. The enzyme showed a maximum activity at pH 7.2 at 30 oC and was stable in the range of pH 6.0-7.5 and the temperature of 10oC - 40oC.
Publication order reference
I. Maliszewska, Institute of Organic Chemistry, Biochemistry and Biotechnology, Technical University, 50-370 Wroclaw, Wybrzeze Wyspianskiego St. 27, Poland