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Summary  Sustainable production of biofuels from lignocellulose feedstocks depends on cheap enzymes for degradation of such biomass. Plants offer a safe and cost‐effective production platform for biopharmaceuticals, vaccines and industrial enzymes boosting biomass conversion to biofuels. Production of intact and functional protein is a prerequisite for large‐scale protein production, and extensive host‐specific post‐translational modifications ( PTM s) often affect the catalytic properties and stability of recombinant enzymes. Here we investigated the impact of plant  PTM s on enzyme performance and stability of the major cellobiohydrolase  Tr Cel7A from  Trichoderma reesei , an industrially relevant enzyme.  Tr Cel7A was produced in  Nicotiana benthamiana  using a vacuum‐based transient expression technology, and this recombinant enzyme ( Tr Cel7A rec ) was compared with the native fungal enzyme ( Tr Cel7A nat ) in terms of  PTM s and catalytic activity on commercial and industrial substrates. We show that the N‐terminal glutamate of  Tr Cel7A rec  was correctly processed by  N. benthamiana  to a pyroglutamate, critical for protein structure, while the linker region of  Tr Cel7A rec  was vulnerable to proteolytic digestion during protein production due to the absence of  O ‐mannosylation in the plant host as compared with the native protein. In general, the purified full‐length  Tr Cel7A rec  had 25% lower catalytic activity than  Tr Cel7A nat  and impaired substrate‐binding properties, which can be attributed to larger  N ‐glycans and lack of  O ‐glycans in  Tr Cel7A rec . All in all, our study reveals that the glycosylation machinery of  N. benthamiana  needs tailoring to optimize the production of efficient cellulases.

plant biotechnology journal

In‐depth characterization of  Trichoderma reesei  cellobiohydrolase  Tr Cel7A produced in  Nicotiana benthamiana  reveals limitations of cellulase production in plants by host‐specific post‐translational modifications