Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from <i>Trichoderma atroviride</i>, <i>T. reesei</i> and <i>T. harzianum</i>.
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| Abstract | :
The ascomycete fungus Trichoderma reesei is the predominant source of enzymes for industrial conversion of lignocellulose. Its glycoside hydrolase family 7 cellobiohydrolase (GH7 CBH) TreCel7A constitutes nearly half of the enzyme cocktail by weight and is the major workhorse in the cellulose hydrolysis process. The orthologs from Trichoderma atroviride (TatCel7A) and Trichoderma harzianum (ThaCel7A) show high sequence identity with TreCel7A, ~ 80%, and represent naturally evolved combinations of cellulose-binding tunnel-enclosing loop motifs, which have been suggested to influence intrinsic cellobiohydrolase properties, such as endo-initiation, processivity, and off-rate. |
| Year of Publication | :
0
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| Journal | :
Biotechnology for biofuels
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| Volume | :
11
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| Number of Pages | :
5
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| Date Published | :
2018
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| URL | :
https://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-017-1006-7
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| DOI | :
10.1186/s13068-017-1006-7
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| Short Title | :
Biotechnol Biofuels
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