Abstract
The extracellular enzymes produced by Trichoderma reesei strain CL847 were submitted to fast protein liquid chromatography on a Mono Q anio-exchange column. Fourteen distinct peaks were separated and characterized by their protein contents and enzymatic activities. The three main peaks were subjected to a second separation on a Mono S cation-exchange column. Except for the cellobiohydrolase II and an endo-β-1,4-glucanase which could not be separated, all the components of the cellulase complex, five other endo-1,4-β- d-glucanases, the cellobiohydrolase I and the β-glucosidase, were purified almost to homogeneity. The fast and reproducible resolutions obtained allowed the design of a routine test for the characterization of mutant strains of T. reesei. Moreover the two-step purification procedure was successfully extrapolated to the preparative scale.
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