학술논문
Detection and partial purification of two lipases fromCandida rugosa
Document Type
Article
Source
Biotechnology Letters; May 1989, Vol. 11 Issue: 5 p345-348, 4p
Subject
Language
ISSN
01415492; 15736776
Abstract
Two distinct lipases produced byCanadida rugosawere 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.