Rapid purification procedure and characterisation of two 1,4-β-D-glucanases from Trichoderma reesei

1992 
Two 1,4-β-D-glucanases were purified to homogeneity from a cellulase preparation originating from Trichoderma reesei, in a two-step chromatographic procedure: anion exchange chromatography on DEAE-Sepharose CL-6B and gel permeation chromatography on Sephacryl S200. The first cellulase was an endoglucanase with high activity on CM-cellulose. These enzymes appeared as homogeneous proteins in SDS-PAGE and in isoelectric focusing; their respective molecular weights were 25,800 and 36,000
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