Abstract
Crude cellulolytic enzyme complexes from Trichoderma reesei QM 9414 and its high-cellulase producing mutants were analyzed by means of analytical isoelectric focusing in polyacrylamide gel cylinders and in flat bed gels. Variations in the peptide composition of individual cellulase preparations as well as in the composition and relative abundance of endo-β- d-1,4-glucanase and β-glucosidase components in the individual cellulase preparations were detected.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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