Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases

Jenni Rahikainen, Ulla Moilanen, Susanna Nurmi-Rantala, Angelos Lappas, Anu Koivula, Liisa Viikari, Kristiina Kruus (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    44 Citations (Scopus)


    Non-productive enzyme adsorption onto lignin inhibits enzymatic hydrolysis of lignocellulosic biomass. Three cellobiohydrolases, Trichoderma reesei Cel7A (TrCel7A) and two engineered fusion enzymes, with distinctive modular structures and temperature stabilities were employed to study the effect of temperature on inhibition arising from non-productive cellulase adsorption. The fusion enzymes, TeCel7A-CBM1 and TeCel7A-CBM3, were composed of a thermostable Talaromyces emersonii Cel7A (TeCel7A) catalytic domain fused to a carbohydrate-binding module (CBM) either from family 1 or from family 3. With all studied enzymes, increase in temperature was found to increase the inhibitory effect of supplemented lignin in the enzymatic hydrolysis of microcrystalline cellulose. However, for the different enzymes, lignin-derived inhibition emerged at different temperatures. Low binding onto lignin and thermostable structure were characteristic for the most lignin-tolerant enzyme, TeCel7A-CBM1, whereas TrCel7A was most susceptible to lignin especially at elevated temperature (55 °C).
    Original languageEnglish
    Pages (from-to)118-125
    JournalBioresource Technology
    Publication statusPublished - 2013
    MoE publication typeA1 Journal article-refereed


    • adsorption
    • cellulase
    • enzymatic hydrolysis
    • enzyme stability
    • lignin


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