Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain: Action on bacterial microcrystalline cellulose

Malee Srisodsuk, Janne Lehtiö, Markus Linder, Emilio Margolles-Clark, Tapani Reinikainen, Tuula Teeri (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Cellulolytic enzymes consist of distinct catalytic and cellulose-binding domains (CBDs). The presence of a CBD improves the binding and activity of cellulases on insoluble substrates but has no influence on their activities on soluble substrates. Structural and biochemical studies of a fungal CBD from Trichoderma reesei cellobiohydrolase I have revealed a wedge shaped structure with a flat cellulose binding surface containing three essential tyrosine residues. The face of the wedge is strictly conserved in all fungal CBDs while many differences occur on the other face of the wedge. Here we have studied the importance of these differences on the function of the T. reesei CBHI by replacing its CBD by a homologous CBD from the endoglucanase, EGI. Our data shows that, apart from slightly improved affinity of the hybrid enzyme, the domain exchange does not significantly influence the function of CBHI.

Original languageEnglish
Pages (from-to)49 - 57
Number of pages9
JournalJournal of Biotechnology
Volume57
Issue number1 - 3
DOIs
Publication statusPublished - 1997
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Trichoderma
Cellulase
Cellulose
Enzymes
Cellulases
Substrates
microcrystalline cellulose
Tyrosine

Cite this

Srisodsuk, Malee ; Lehtiö, Janne ; Linder, Markus ; Margolles-Clark, Emilio ; Reinikainen, Tapani ; Teeri, Tuula. / Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain : Action on bacterial microcrystalline cellulose. In: Journal of Biotechnology. 1997 ; Vol. 57, No. 1 - 3. pp. 49 - 57.
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abstract = "Cellulolytic enzymes consist of distinct catalytic and cellulose-binding domains (CBDs). The presence of a CBD improves the binding and activity of cellulases on insoluble substrates but has no influence on their activities on soluble substrates. Structural and biochemical studies of a fungal CBD from Trichoderma reesei cellobiohydrolase I have revealed a wedge shaped structure with a flat cellulose binding surface containing three essential tyrosine residues. The face of the wedge is strictly conserved in all fungal CBDs while many differences occur on the other face of the wedge. Here we have studied the importance of these differences on the function of the T. reesei CBHI by replacing its CBD by a homologous CBD from the endoglucanase, EGI. Our data shows that, apart from slightly improved affinity of the hybrid enzyme, the domain exchange does not significantly influence the function of CBHI.",
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Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain : Action on bacterial microcrystalline cellulose. / Srisodsuk, Malee; Lehtiö, Janne; Linder, Markus; Margolles-Clark, Emilio; Reinikainen, Tapani; Teeri, Tuula (Corresponding Author).

In: Journal of Biotechnology, Vol. 57, No. 1 - 3, 1997, p. 49 - 57.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain

T2 - Action on bacterial microcrystalline cellulose

AU - Srisodsuk, Malee

AU - Lehtiö, Janne

AU - Linder, Markus

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AU - Teeri, Tuula

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AB - Cellulolytic enzymes consist of distinct catalytic and cellulose-binding domains (CBDs). The presence of a CBD improves the binding and activity of cellulases on insoluble substrates but has no influence on their activities on soluble substrates. Structural and biochemical studies of a fungal CBD from Trichoderma reesei cellobiohydrolase I have revealed a wedge shaped structure with a flat cellulose binding surface containing three essential tyrosine residues. The face of the wedge is strictly conserved in all fungal CBDs while many differences occur on the other face of the wedge. Here we have studied the importance of these differences on the function of the T. reesei CBHI by replacing its CBD by a homologous CBD from the endoglucanase, EGI. Our data shows that, apart from slightly improved affinity of the hybrid enzyme, the domain exchange does not significantly influence the function of CBHI.

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