The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei
The origin of these studies from our interest in the use of protein denaturants to elute cellulase enzyme components from residual cellulosic substrates. A high concentration of the denaturant guanidine hydrochloride, required for elution, was found to only partially unfold the major component of T....
| Main Authors: | , |
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| Language: | unknown |
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2022
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| Subjects: | |
| Online Access: | http://www.osti.gov/servlets/purl/6602610 https://www.osti.gov/biblio/6602610 |
| Summary: | The origin of these studies from our interest in the use of protein denaturants to elute cellulase enzyme components from residual cellulosic substrates. A high concentration of the denaturant guanidine hydrochloride, required for elution, was found to only partially unfold the major component of T. reesei cellulase, cellobiohydrolase I(CBH I), and that the reason for the loss in catalytic activity was due to the competitive inhibition of this enzyme and not, as expected, due to its unfolding or denaturation. Papain digestion of CBH I generated core'' enzyme which, apparently, completely broke up upon reduction. These data are discussed in relation to structure/function relationships of this key cellulase enzyme component. In this paper studies on the effect of denaturation and reduction of CBH I are described. The rationale for these studies is to further our understanding of the structure and function relationships of this key cellulase enzyme and to determine the methodology for its successful unfolding and refolding that may be necessary for its recovery. 18 refs., 5 figs. |
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