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

Jenni Rahikainen, U Moilanen, Susanna Nurmi-Rantala, A. Lappas, Anu Koivula, L. Viikari, Kristiina Kruus (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

29 Citations (Scopus)

Abstract

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
Number of pages7
JournalBioresource Technology
Volume146
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Lignin
lignin
Enzymes
enzyme
Enzymatic hydrolysis
temperature
Temperature
hydrolysis
Fusion reactions
adsorption
Enzyme inhibition
Adsorption
Cellulase
Carbohydrates
effect
cellulose
carbohydrate
Cellulose
Biomass

Keywords

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

Cite this

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title = "Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases",
abstract = "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).",
keywords = "adsorption, cellulase, enzymatic hydrolysis, enzyme stability, lignin",
author = "Jenni Rahikainen and U Moilanen and Susanna Nurmi-Rantala and A. Lappas and Anu Koivula and L. Viikari and Kristiina Kruus",
year = "2013",
doi = "10.1016/j.biortech.2013.07.069",
language = "English",
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pages = "118--125",
journal = "Bioresource Technology",
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Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases. / Rahikainen, Jenni; Moilanen, U; Nurmi-Rantala, Susanna; Lappas, A.; Koivula, Anu; Viikari, L.; Kruus, Kristiina (Corresponding Author).

In: Bioresource Technology, Vol. 146, 2013, p. 118-125.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases

AU - Rahikainen, Jenni

AU - Moilanen, U

AU - Nurmi-Rantala, Susanna

AU - Lappas, A.

AU - Koivula, Anu

AU - Viikari, L.

AU - Kruus, Kristiina

PY - 2013

Y1 - 2013

N2 - 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).

AB - 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).

KW - adsorption

KW - cellulase

KW - enzymatic hydrolysis

KW - enzyme stability

KW - lignin

U2 - 10.1016/j.biortech.2013.07.069

DO - 10.1016/j.biortech.2013.07.069

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JF - Bioresource Technology

SN - 0960-8524

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