Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin

Hetti Palonen (Corresponding Author), Folke Tjerneld, Guido Zacchi, Maija Tenkanen

Research output: Contribution to journalArticleScientificpeer-review

351 Citations (Scopus)

Abstract

The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG II or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG II also bound to isolated lignin. Surprisingly, the catalytic domains of the two enzymes of T. reesei differed essentially in the adsorption to isolated lignin. The catalytic domain of EG II was able to adsorb to alkaline isolated lignin with a high affinity, whereas the catalytic domain of CBH I did not adsorb to any of the lignins tested. The results indicate that the cellulose binding domain has a significant role in the unspecific binding of cellulases to lignin.
Original languageEnglish
Pages (from-to)65-72
JournalJournal of Biotechnology
Volume107
Issue number1
DOIs
Publication statusPublished - 2004
MoE publication typeA1 Journal article-refereed

Fingerprint

Trichoderma
Softwoods
Lignin
Steam
Adsorption
Catalytic Domain
Cellulases
Enzymes
Cellulose
Enzymatic hydrolysis
Tritium
Hydrolysis
Degradation

Keywords

  • Lignocellulose
  • Lignin
  • Adsorption
  • Cellulase
  • Trichoderma reesei

Cite this

Palonen, Hetti ; Tjerneld, Folke ; Zacchi, Guido ; Tenkanen, Maija. / Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin. In: Journal of Biotechnology. 2004 ; Vol. 107, No. 1. pp. 65-72.
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Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin. / Palonen, Hetti (Corresponding Author); Tjerneld, Folke; Zacchi, Guido; Tenkanen, Maija.

In: Journal of Biotechnology, Vol. 107, No. 1, 2004, p. 65-72.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin

AU - Palonen, Hetti

AU - Tjerneld, Folke

AU - Zacchi, Guido

AU - Tenkanen, Maija

PY - 2004

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N2 - The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG II or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG II also bound to isolated lignin. Surprisingly, the catalytic domains of the two enzymes of T. reesei differed essentially in the adsorption to isolated lignin. The catalytic domain of EG II was able to adsorb to alkaline isolated lignin with a high affinity, whereas the catalytic domain of CBH I did not adsorb to any of the lignins tested. The results indicate that the cellulose binding domain has a significant role in the unspecific binding of cellulases to lignin.

AB - The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG II or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG II also bound to isolated lignin. Surprisingly, the catalytic domains of the two enzymes of T. reesei differed essentially in the adsorption to isolated lignin. The catalytic domain of EG II was able to adsorb to alkaline isolated lignin with a high affinity, whereas the catalytic domain of CBH I did not adsorb to any of the lignins tested. The results indicate that the cellulose binding domain has a significant role in the unspecific binding of cellulases to lignin.

KW - Lignocellulose

KW - Lignin

KW - Adsorption

KW - Cellulase

KW - Trichoderma reesei

U2 - 10.1016/j.jbiotec.2003.09.011

DO - 10.1016/j.jbiotec.2003.09.011

M3 - Article

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JF - Journal of Biotechnology

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