Publikasjoner
NIBIOs ansatte publiserer flere hundre vitenskapelige artikler og forskningsrapporter hvert år. Her finner du referanser og lenker til publikasjoner og andre forsknings- og formidlingsaktiviteter. Samlingen oppdateres løpende med både nytt og historisk materiale. For mer informasjon om NIBIOs publikasjoner, besøk NIBIOs bibliotek.
2019
Sammendrag
Det er ikke registrert sammendrag
Sammendrag
Det er ikke registrert sammendrag
Forfattere
Knut-Erik Tollefsen Karina Petersen Ana Catarina Almeida Thomas Backhaus Tania Gomes H.R. Norli Sven R. Odenmarck Hans Ragnar Norli You Song Raoul Wolf Li Xie Joachim Sturve Marianne StenrødSammendrag
Det er ikke registrert sammendrag
Sammendrag
Det er ikke registrert sammendrag
Forfattere
Eva Narten HøbergSammendrag
Det er ikke registrert sammendrag
Sammendrag
Det er ikke registrert sammendrag
Forfattere
Eva Narten HøbergSammendrag
Det er ikke registrert sammendrag
Sammendrag
Det er ikke registrert sammendrag
Sammendrag
Det er ikke registrert sammendrag
Forfattere
Andre van Eerde Aniko Varnai John-Kristian Jameson Lisa Paruch Anders Moen Jan Haug Anonsen Piotr Chylenski Hege Særvold Steen Inger Heldal Ralph Bock Vincent Eijsink Jihong Liu ClarkeSammendrag
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 (PTMs) often affect the catalytic properties and stability of recombinant enzymes. Here we investigated the impact of plant PTMs on enzyme performance and stability of the major cellobiohydrolase TrCel7A from Trichoderma reesei, an industrially relevant enzyme. TrCel7A was produced in Nicotiana benthamiana using a vacuum‐based transient expression technology, and this recombinant enzyme (TrCel7Arec) was compared with the native fungal enzyme (TrCel7Anat) in terms of PTMs and catalytic activity on commercial and industrial substrates. We show that the N‐terminal glutamate of TrCel7Arec was correctly processed by N. benthamiana to a pyroglutamate, critical for protein structure, while the linker region of TrCel7Arec 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 TrCel7Arec had 25% lower catalytic activity than TrCel7Anat and impaired substrate‐binding properties, which can be attributed to larger N‐glycans and lack of O‐glycans in TrCel7Arec. All in all, our study reveals that the glycosylation machinery of N. benthamiana needs tailoring to optimize the production of efficient cellulases.