Abstract
Cell growth of Trichoderma reesei is greatly inhibited by furan derivatives (furfural and HMF) generated during pretreatment of lignocellulose, and the cellulase production is hence suppressed. In this study, a novel recombinant strain of T. reesei with high tolerance to furans was constructed by homologously co-expressing nicotinate phosphoribosyltransferase and alcohol dehydrogenase. We observed that furfural had a stronger inhibitory effect than HMF and cellulase production was decreased by 35% in T. reesei with the stress of 2.5 mM furfural. The activities of nicotinate phosphoribosyltransferase and alcohol dehydrogenase increased 8.6-fold and 2.9-fold in the recombinant strain, respectively. Furfural was effectively converted into furfuryl alcohol which was then depleted, thus the production of cellulase could be recovered when the recombinant strain was grown in 5% (w/v) two-step stem explosion pretreated rice straw without detoxification. This work presents an important strategy for efficient enzyme production in T. reesei from non-detoxified pretreated lignocellulose feedstocks.
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