Analysis of cellulase proteins by high-performance liquid chromatography.
A new procedure using high-performance liquid chromatography for the rapid separation of cellulase proteins is described. The cellulase components of Trichoderma reesei are fractionated on a DEAE anion-exchange column using a phosphate buffer at pH 6.2. Activities of the individual components obtained from T. reesei QM6a, a wild strain, and several mutant strains have been determined. Each system examined contained beta-glucosidase, at least two exo-beta-1,4 glucanases and five endo-beta-1,4 glucanases with the endo-beta-1,4 glucanases accounting for 20--36% and the exo-beta-1,4 glucanases for 64--80% of the soluble protein.
D002480:Cellulase / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D003904:Mitosporic Fungi / Q000201:enzymology*; D009154:Mutation; D013045:Species Specificity; D014242:Trichoderma / Q000201:enzymology*
D002480:Cellulase