@misc{Maliszewska_Irena_H._Purification_1997,
 author={Maliszewska, Irena H.},
 volume={38},
 number={3},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.38, 3 (1997)-.},
 howpublished={online},
 year={1997},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 abstract={An extracellular lipase (glycerol ester hydrolases E.C. 3.1.1.3.) was isolated from a culturefiltrate of Penicillium citńnum. The purification procedure included ammonium sulfate precipitation, ultrafiltration and chromatography on Octyl-Sepharose CL-4B. The enzyme was 400-foldpurified with 9.66% yield. The molecular weight has been estimated by polyacrylamide gel electrophoresis under denaturing conditions at 26 000. On the other hand, lipase forms active dimersand tetramers aggregates as observed after native PAGE. Lipase from Penicillium citrinum showeda preference for triacylglycerols. It is non-specific and hydrolyzes each of the three ester bondsof triacylglycerols. The enzyme showed a maximum activity at pH 7.2 at 30°C and was stablein the range of pH 6.0-7.5 and the temperature of 10°C - 40°C.},
 title={Purification and some characteristics of Penicillium citrinum lipase},
 type={Text},
 URL={http://rcin.org.pl./Content/146003/PDF/POZN271_181196_biotechnologia-1997-no3-maliszewska.pdf},
 keywords={biotechnology},
}