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Purification and some characteristics of Penicillium citrinum lipase
Subtitle:Purification and some characteristics of Penicillium citrinum lipase
Creator: Publisher:Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
Date issued/created: Type of object: Subject and Keywords: 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.
Relation:Biotechnologia, vol.38, 3 (1997)-.
Volume: Issue: Start page: End page: Resource type: Detailed Resource Type: Format: Resource Identifier: Source:Library of Institute of Bioorganic Chemistry PAS
Language: Language of abstract: Temporal coverage: Rights:Creative Commons Attribution BY-SA 4.0 license
Terms of use: Digitizing institution:Institute of Bioorganic Chemistry of the Polish Academy of Science
Original in:Institute of Bioorganic Chemistry of the Polish Academy of Science
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