ABSTRACT
Lactose (1,4-
O
-β-
d
-galacto-pyranosyl-
d
-glucose) induces cellulolytic enzymes in
Trichoderma reesei
and is in fact one of the most important soluble carbon sources used to produce cellulases on an industrial level. The mechanism underlying the induction is, however, not fully understood. In this study, we investigated the cellular functions of the intracellular β-glucosidases CEL1a and CEL1b in the induction of cellulase genes by lactose in
T. reesei
. We demonstrated that while CEL1a and CEL1b were functionally equivalent in mediating the induction, the simultaneous absence of these intracellular β-glucosidases abolished
cbh1
gene expression on lactose.
d
-Galactose restored the efficient cellulase gene induction in the Δ
cel1a
strain independently of its reductive metabolism, but not in the Δ
cel1a
Δ
cel1b
strain. A further comparison of the transcriptional responses of the Δ
cel1a
Δ
cel1b
strain complemented with wild-type CEL1a or a catalytically inactive CEL1a version and the Δ
cel1a
strain constitutively expressing CEL1a or the
Kluyveromyces lactis
β-galactosidase LAC4 showed that both the CEL1a protein and its glycoside hydrolytic activity were indispensable for cellulase induction by lactose. We also present evidence that intracellular β-glucosidase-mediated lactose induction is further conveyed to XYR1 to ensure the efficiently induced expression of cellulase genes.