Fig. 6

Cellulolytic activities of purified T. reesei CBH I secreted by T. reesei and chimeric TeTrCBH I secreted by L. starkeyi. The enzyme cocktails consisted of CBH I (either T. reesei CBH I or chimeric TeTrCBH I; 28 mg/g substrate), A. cellulolyticus E1-CAT (Y245G) (1.89 mg/g substrate) and A. niger β-d-glucosidase (0.50 mg/g substrate). The substrate used for these assays was pretreated corn stover loaded at 5 mg/mL in 20 mM acetate buffer pH 5.0 and the assay temperature was 40 °C. T. reesei CBH I was purified from the native host; chimeric TeTrCBH I is the Talaromyces emersonii CBH I catalytic domain fused to the linker and CBM from T. reesei CBH I and was expressed in L. starkeyi guided by the signal peptide of L. starkeyi dextranase II. βG is the β-d-glucosidase purified from A. niger; and E1-CAT (Y245G) is the engineered A. cellulolyticus endocellulase E1 catalytic domain