Abstract
The lipase of Chromobacterium viscosum in the crude enzyme preparation was specifically adsorbed on glass beads coated with various hydrophobic materials. The enzyme adsorbed on siliconized glass beads was not denatured and eluted with 0.1% Triton X-100 and other detergents. The adsorptive nature of lipase on hydrophobic glass beads was applied to its purification by a one-step process. As the result, lipases of Chromobacterium, Pseudomonas, Candida, and Rhizopus were purified 300-, 670, 160-, and 110-fold, respectively. The lipases purified from Chromobacterium and Candida were examined by disc electrophoresis, and they were judged to be of high purity. Purification of the lipase from Chromobacterium by a column method with siliconized glass beads confirmed that this method allowed about 1000-fold purification.
