Purification of Two Avicelases from Aspergillus aculeatus No. F-50 |
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| Authors: | Sawao Murao Reiichiro Sakamoto Motoo Arai |
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| Institution: | 1. Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture, Sakai, Osaka 591, Japan;2. Japan Pulp &3. Paper Research Institute, Inc., Tokodai, Toyosatomachi Tsukubagun, Ibaraki 300–26, Japan |
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| Abstract: | An assay system for cellulases which are active on microcrystalline cellulose (Avicel) has been designed, that is, the cellulase activity was effectively assayed in the presence of endo-glucanase and β-glucosidase. Using this system, two electrophoretically distinct cellulases, which are called FI-Avicelase and FIII-Avicelase, have been purified from the culture filtrate of Aspergillus aculeatus No. F-50 to homogeneity by DEAE- and SP-Sephadex column chromatographies, and gel filtration with Sephacryl S-200. The molecular weights of the FI- and FIII-Avicelases were estimated to be 109,000 and 112,000, respectively, and their isoelectric points to be 4.7 and 4.0. Both cellulases are glycoproteins containing 20 to 30% sugar, but they differ from each other in amino acid composition. |
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