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....
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ftosti:oai:osti.gov:6602610 2023-07-30T04:02:56+02:00 The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei Woodward, J. ) Herrmann, P.C. ) 2022-10-17 application/pdf http://www.osti.gov/servlets/purl/6602610 https://www.osti.gov/biblio/6602610 unknown http://www.osti.gov/servlets/purl/6602610 https://www.osti.gov/biblio/6602610 59 BASIC BIOLOGICAL SCIENCES HYDROLASES PROTEIN DENATURATION BIOLOGICAL EFFECTS BIOASSAY CELLULASE CELLULOSE DIGESTION ENZYMATIC HYDROLYSIS ENZYME INHIBITORS GUANIDINES PAPAIN PURIFICATION REDUCTION TRICHODERMA CARBOHYDRATES CARBONIC ACID DERIVATIVES CHEMICAL REACTIONS DECOMPOSITION ENZYMES EUMYCOTA FUNGI GLYCOSYL HYDROLASES HYDROLYSIS LYSIS O-GLYCOSYL HYDROLASES ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS PEPTIDE HYDROLASES PLANTS POLYSACCHARIDES SACCHARIDES SH-PROTEINASES SOLVOLYSIS 2022 ftosti 2023-07-11T10:50:02Z 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. Other/Unknown Material Carbonic acid SciTec Connect (Office of Scientific and Technical Information - OSTI, U.S. Department of Energy) |
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SciTec Connect (Office of Scientific and Technical Information - OSTI, U.S. Department of Energy) |
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topic |
59 BASIC BIOLOGICAL SCIENCES HYDROLASES PROTEIN DENATURATION BIOLOGICAL EFFECTS BIOASSAY CELLULASE CELLULOSE DIGESTION ENZYMATIC HYDROLYSIS ENZYME INHIBITORS GUANIDINES PAPAIN PURIFICATION REDUCTION TRICHODERMA CARBOHYDRATES CARBONIC ACID DERIVATIVES CHEMICAL REACTIONS DECOMPOSITION ENZYMES EUMYCOTA FUNGI GLYCOSYL HYDROLASES HYDROLYSIS LYSIS O-GLYCOSYL HYDROLASES ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS PEPTIDE HYDROLASES PLANTS POLYSACCHARIDES SACCHARIDES SH-PROTEINASES SOLVOLYSIS |
spellingShingle |
59 BASIC BIOLOGICAL SCIENCES HYDROLASES PROTEIN DENATURATION BIOLOGICAL EFFECTS BIOASSAY CELLULASE CELLULOSE DIGESTION ENZYMATIC HYDROLYSIS ENZYME INHIBITORS GUANIDINES PAPAIN PURIFICATION REDUCTION TRICHODERMA CARBOHYDRATES CARBONIC ACID DERIVATIVES CHEMICAL REACTIONS DECOMPOSITION ENZYMES EUMYCOTA FUNGI GLYCOSYL HYDROLASES HYDROLYSIS LYSIS O-GLYCOSYL HYDROLASES ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS PEPTIDE HYDROLASES PLANTS POLYSACCHARIDES SACCHARIDES SH-PROTEINASES SOLVOLYSIS Woodward, J. ) Herrmann, P.C. ) The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei |
topic_facet |
59 BASIC BIOLOGICAL SCIENCES HYDROLASES PROTEIN DENATURATION BIOLOGICAL EFFECTS BIOASSAY CELLULASE CELLULOSE DIGESTION ENZYMATIC HYDROLYSIS ENZYME INHIBITORS GUANIDINES PAPAIN PURIFICATION REDUCTION TRICHODERMA CARBOHYDRATES CARBONIC ACID DERIVATIVES CHEMICAL REACTIONS DECOMPOSITION ENZYMES EUMYCOTA FUNGI GLYCOSYL HYDROLASES HYDROLYSIS LYSIS O-GLYCOSYL HYDROLASES ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS PEPTIDE HYDROLASES PLANTS POLYSACCHARIDES SACCHARIDES SH-PROTEINASES SOLVOLYSIS |
description |
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. |
author |
Woodward, J. ) Herrmann, P.C. ) |
author_facet |
Woodward, J. ) Herrmann, P.C. ) |
author_sort |
Woodward, J. ) |
title |
The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei |
title_short |
The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei |
title_full |
The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei |
title_fullStr |
The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei |
title_full_unstemmed |
The effect of denaturation and reduction on cellobiohydrolase 1 from Trichoderma reesei |
title_sort |
effect of denaturation and reduction on cellobiohydrolase 1 from trichoderma reesei |
publishDate |
2022 |
url |
http://www.osti.gov/servlets/purl/6602610 https://www.osti.gov/biblio/6602610 |
genre |
Carbonic acid |
genre_facet |
Carbonic acid |
op_relation |
http://www.osti.gov/servlets/purl/6602610 https://www.osti.gov/biblio/6602610 |
_version_ |
1772813816642404352 |