Analysis of cellulase proteins by high-performance liquid chromatography.

Abstract A new procedure using high-performance liquid chromatography for the rapid separation of cellulase proteins is described. The cellulase components ot 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 β-glucosidase, at least two exo -β-1,4 glucanases and five endo -β-1,4 glucanases with the endo -β-1,4 glucanases accounting for 20–36% and the exo -β-1,4 glucanases for 64–80% of the soluble protein.