Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases.
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).
VTT Technical Research Centre of Finland, P.O. Box 1000, 02044 VTT, Finland.
Jenni Liisa
JL
Rahikainen
University of Helsinki, P.O. Box 27, 00014 University of Helsinki, Helsinki, Finland.
Ulla
U
Moilanen
VTT Technical Research Centre of Finland, P.O. Box 1000, 02044 VTT, Finland.
Susanna
S
Nurmi-Rantala
Center for Research and Technology Hellas (CERTH), Chemical Process Engineering Research Institute, P.O. Box 60361, 57001 Thermi-Thessaloniki, Greece.
Angelos
A
Lappas
VTT Technical Research Centre of Finland, P.O. Box 1000, 02044 VTT, Finland.
Anu
A
Koivula
University of Helsinki, P.O. Box 27, 00014 University of Helsinki, Helsinki, Finland.
Liisa
L
Viikari
VTT Technical Research Centre of Finland, P.O. Box 1000, 02044 VTT, Finland. Electronic address: kristiina.kruus@vtt.fi.
Kristiina
K
Kruus
D000327:Adsorption; D001673:Biodegradation, Environmental; D018533:Biomass; D002241:Carbohydrates / Q000737:chemistry; D020134:Catalytic Domain; D002480:Cellulase / Q000737:chemistry; D002482:Cellulose / Q000737:chemistry; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000737:chemistry*; D003460:Crystallization; D006868:Hydrolysis; D008031:Lignin / Q000737:chemistry*; D013696:Temperature; D013997:Time Factors; D014242:Trichoderma / Q000378:metabolism; D014908:Triticum; D014934:Wood
D002241:Carbohydrates; C036909:lignocellulose; D002482:Cellulose; D008031:Lignin; D002480:Cellulase; D043366:Cellulose 1,4-beta-Cellobiosidase
Adsorption; Cellulase; Enzymatic hydrolysis; Enzyme stability; Lignin