Modes of action on cotton and bacterial cellulose of a homologous endoglucanase-exoglucanase pair from Trichoderma reesei

Malee Srisodsuk, Karen Kleman-Leyer, Sirkka Keränen, T. Kent Kirk, Tuula Teeri (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

The endoglucanase I (EGI) and the cellobiohydrolase I (CBHI) of the filamentous fungus Trichoderma reesei form a homologous pair of cellulolytic enzymes which nevertheless have different modes of action.
We show here that the action of CBHI on bacterial microcrystalline cellulose results in efficient solubilisation but only a slow decrease in its degree of polymerisation. In contrast, the action of EGI results in a rapid decrease of the degree of polymerisation but less efficient overall solubilisation of the substrate. CBHI alone was practically inactive toward cotton which has a high initial degree of polymerisation and a complex morphology.
EGI rapidly reduced the degree of polymerisation of cotton, and slowly solubilised part of it. Working synergistically, EGI and CBHI solubilised cotton more rapidly and to a greater extent than EGI alone.
Our data are consistent with the exoglucanase nature of CBHI and also provide some evidence supporting its processive mode of action.
Original languageEnglish
Pages (from-to)885-892
JournalEuropean Journal of Biochemistry
Volume251
Issue number3
DOIs
Publication statusPublished - 1998
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Cellulases
Trichoderma
Cellulase
Cellulose
Cotton
Polymerization
Fungi
Substrates
Enzymes

Cite this

Srisodsuk, Malee ; Kleman-Leyer, Karen ; Keränen, Sirkka ; Kirk, T. Kent ; Teeri, Tuula. / Modes of action on cotton and bacterial cellulose of a homologous endoglucanase-exoglucanase pair from Trichoderma reesei. In: European Journal of Biochemistry. 1998 ; Vol. 251, No. 3. pp. 885-892.
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abstract = "The endoglucanase I (EGI) and the cellobiohydrolase I (CBHI) of the filamentous fungus Trichoderma reesei form a homologous pair of cellulolytic enzymes which nevertheless have different modes of action. We show here that the action of CBHI on bacterial microcrystalline cellulose results in efficient solubilisation but only a slow decrease in its degree of polymerisation. In contrast, the action of EGI results in a rapid decrease of the degree of polymerisation but less efficient overall solubilisation of the substrate. CBHI alone was practically inactive toward cotton which has a high initial degree of polymerisation and a complex morphology. EGI rapidly reduced the degree of polymerisation of cotton, and slowly solubilised part of it. Working synergistically, EGI and CBHI solubilised cotton more rapidly and to a greater extent than EGI alone. Our data are consistent with the exoglucanase nature of CBHI and also provide some evidence supporting its processive mode of action.",
author = "Malee Srisodsuk and Karen Kleman-Leyer and Sirkka Ker{\"a}nen and Kirk, {T. Kent} and Tuula Teeri",
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Modes of action on cotton and bacterial cellulose of a homologous endoglucanase-exoglucanase pair from Trichoderma reesei. / Srisodsuk, Malee; Kleman-Leyer, Karen; Keränen, Sirkka; Kirk, T. Kent; Teeri, Tuula (Corresponding Author).

In: European Journal of Biochemistry, Vol. 251, No. 3, 1998, p. 885-892.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Modes of action on cotton and bacterial cellulose of a homologous endoglucanase-exoglucanase pair from Trichoderma reesei

AU - Srisodsuk, Malee

AU - Kleman-Leyer, Karen

AU - Keränen, Sirkka

AU - Kirk, T. Kent

AU - Teeri, Tuula

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N2 - The endoglucanase I (EGI) and the cellobiohydrolase I (CBHI) of the filamentous fungus Trichoderma reesei form a homologous pair of cellulolytic enzymes which nevertheless have different modes of action. We show here that the action of CBHI on bacterial microcrystalline cellulose results in efficient solubilisation but only a slow decrease in its degree of polymerisation. In contrast, the action of EGI results in a rapid decrease of the degree of polymerisation but less efficient overall solubilisation of the substrate. CBHI alone was practically inactive toward cotton which has a high initial degree of polymerisation and a complex morphology. EGI rapidly reduced the degree of polymerisation of cotton, and slowly solubilised part of it. Working synergistically, EGI and CBHI solubilised cotton more rapidly and to a greater extent than EGI alone. Our data are consistent with the exoglucanase nature of CBHI and also provide some evidence supporting its processive mode of action.

AB - The endoglucanase I (EGI) and the cellobiohydrolase I (CBHI) of the filamentous fungus Trichoderma reesei form a homologous pair of cellulolytic enzymes which nevertheless have different modes of action. We show here that the action of CBHI on bacterial microcrystalline cellulose results in efficient solubilisation but only a slow decrease in its degree of polymerisation. In contrast, the action of EGI results in a rapid decrease of the degree of polymerisation but less efficient overall solubilisation of the substrate. CBHI alone was practically inactive toward cotton which has a high initial degree of polymerisation and a complex morphology. EGI rapidly reduced the degree of polymerisation of cotton, and slowly solubilised part of it. Working synergistically, EGI and CBHI solubilised cotton more rapidly and to a greater extent than EGI alone. Our data are consistent with the exoglucanase nature of CBHI and also provide some evidence supporting its processive mode of action.

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JF - FEBS Journal

SN - 1742-464X

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