Detection and partial purification of two lipases fromCandida rugosa |
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| Authors: | Veeraragavan Kannappan Gibbs Bernard F |
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| Institution: | (1) Protein Engineering Section, Biotechnology Research Institute, National Research Council of Canada, H4P 2R2 Montreal, Quebec, Canada |
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| Abstract: | Summary Two distinct lipases produced byCanadida rugosa were identified and separated by a high resolution anion-exchange column (Mono Q) after an ethanol extraction of the crude lipase. From this Mono Q column, lipase I eluted at 0.05 M NaCl whereas lipase II eluted at 0.15 M NaCl. The less anionic nature of lipase I was also confirmed by native polyacrylamide gel electrophoresis as well as isoelectrophoresis. Both proteins have an apparent molecular weight of 58,000 by SDS-PAGE. The isoelectric points of lipase I and II are 5.6 and 5.8 respectively. |
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