Hydrolysis of steam-pretreated lignocellulose: synergism and adsorption for cellobiohydrolase I and endoglucanase II of Trichoderma reesei.
Identifieur interne : 001D83 ( Main/Corpus ); précédent : 001D82; suivant : 001D84Hydrolysis of steam-pretreated lignocellulose: synergism and adsorption for cellobiohydrolase I and endoglucanase II of Trichoderma reesei.
Auteurs : J. Karlsson ; J. Medve ; F. TjerneldSource :
- Applied biochemistry and biotechnology [ 0273-2289 ] ; 1999.
Abstract
The mechanism of hydrolysis of cellulose is important for improving the enzymatic conversion in bioprocesses based on lignocellulose. Adsorption and hydrolysis experiments were performed with cellobiohydrolase I (CBH I) and endoglucanase II (EG II) from Trichoderma reesei on a realistic lignocellulose substrates: steam-pretreated willow. The enzymes were studied both alone and in equimolar mixtures. Adsorption isotherms were determined at 4 and 40 degrees C during 90-min reaction times. Both CBH I and EG II adsorbed stronger at 40 than at 4 degrees C. The time course of adsorption and hydrolysis, 3 min to 48 h, was studied at 40 degrees C. About 90% of the cellulases were adsorbed within 2 h. The hydrolysis rate was high in the beginning but decreased during the time course. Based on adsorption data, the hydrolysis and synergism were analyzed as function of adsorbed enzyme. CBH I showed a linear correlation between hydrolysis and adsorbed enzyme, whereas for EG II the corresponding curve leveled off at both 4 and 40 degrees C. At low conversion, below 1%, EG II produced as much soluble sugars as CBH I. At higher conversion, CBH I was more efficient than EG II. The synergism as function of adsorbed enzyme increased with bound enzyme before reaching a stable value of about 2. The effect of varying the ratio of CBH I:EG II was studied at fixed total enzyme loading and by changing the ratio between the enzymes. Only a small addition (5%) of EG II to a CBH I solution was shown to be sufficient for nearly maximal synergism. The ratio between EG II and CBH I was not critical. The ratio 40% EG II:60% CBH I showed similar conversion to 5% EG II:95% CBH I. Modifications of the conventional endo-exo synergism model are proposed.
DOI: 10.1385/abab:82:3:243
PubMed: 15304773
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Tjerneld</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:15304773</idno><idno type="pmid">15304773</idno><idno type="doi">10.1385/abab:82:3:243</idno><idno type="wicri:Area/Main/Corpus">001D83</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001D83</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Hydrolysis of steam-pretreated lignocellulose: synergism and adsorption for cellobiohydrolase I and endoglucanase II of Trichoderma reesei.</title><author><name sortKey="Karlsson, J" sort="Karlsson, J" uniqKey="Karlsson J" first="J" last="Karlsson">J. Karlsson</name><affiliation><nlm:affiliation>Department of Biochemistry, Center for Chemistry and Chemical Engineering, Lund University, PO Box 124, S-221 00 Lund, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Medve, J" sort="Medve, J" uniqKey="Medve J" first="J" last="Medve">J. Medve</name></author><author><name sortKey="Tjerneld, F" sort="Tjerneld, F" uniqKey="Tjerneld F" first="F" last="Tjerneld">F. Tjerneld</name></author></analytic><series><title level="j">Applied biochemistry and biotechnology</title><idno type="ISSN">0273-2289</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mechanism of hydrolysis of cellulose is important for improving the enzymatic conversion in bioprocesses based on lignocellulose. Adsorption and hydrolysis experiments were performed with cellobiohydrolase I (CBH I) and endoglucanase II (EG II) from Trichoderma reesei on a realistic lignocellulose substrates: steam-pretreated willow. The enzymes were studied both alone and in equimolar mixtures. Adsorption isotherms were determined at 4 and 40 degrees C during 90-min reaction times. Both CBH I and EG II adsorbed stronger at 40 than at 4 degrees C. The time course of adsorption and hydrolysis, 3 min to 48 h, was studied at 40 degrees C. About 90% of the cellulases were adsorbed within 2 h. The hydrolysis rate was high in the beginning but decreased during the time course. Based on adsorption data, the hydrolysis and synergism were analyzed as function of adsorbed enzyme. CBH I showed a linear correlation between hydrolysis and adsorbed enzyme, whereas for EG II the corresponding curve leveled off at both 4 and 40 degrees C. At low conversion, below 1%, EG II produced as much soluble sugars as CBH I. At higher conversion, CBH I was more efficient than EG II. The synergism as function of adsorbed enzyme increased with bound enzyme before reaching a stable value of about 2. The effect of varying the ratio of CBH I:EG II was studied at fixed total enzyme loading and by changing the ratio between the enzymes. Only a small addition (5%) of EG II to a CBH I solution was shown to be sufficient for nearly maximal synergism. The ratio between EG II and CBH I was not critical. The ratio 40% EG II:60% CBH I showed similar conversion to 5% EG II:95% CBH I. Modifications of the conventional endo-exo synergism model are proposed.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">15304773</PMID><DateCompleted><Year>2005</Year><Month>02</Month><Day>22</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>11</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0273-2289</ISSN><JournalIssue CitedMedium="Print"><Volume>82</Volume><Issue>3</Issue><PubDate><Year>1999</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Applied biochemistry and biotechnology</Title><ISOAbbreviation>Appl Biochem Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Hydrolysis of steam-pretreated lignocellulose: synergism and adsorption for cellobiohydrolase I and endoglucanase II of Trichoderma reesei.</ArticleTitle><Pagination><MedlinePgn>243-58</MedlinePgn></Pagination><Abstract><AbstractText>The mechanism of hydrolysis of cellulose is important for improving the enzymatic conversion in bioprocesses based on lignocellulose. Adsorption and hydrolysis experiments were performed with cellobiohydrolase I (CBH I) and endoglucanase II (EG II) from Trichoderma reesei on a realistic lignocellulose substrates: steam-pretreated willow. The enzymes were studied both alone and in equimolar mixtures. Adsorption isotherms were determined at 4 and 40 degrees C during 90-min reaction times. Both CBH I and EG II adsorbed stronger at 40 than at 4 degrees C. The time course of adsorption and hydrolysis, 3 min to 48 h, was studied at 40 degrees C. About 90% of the cellulases were adsorbed within 2 h. The hydrolysis rate was high in the beginning but decreased during the time course. Based on adsorption data, the hydrolysis and synergism were analyzed as function of adsorbed enzyme. CBH I showed a linear correlation between hydrolysis and adsorbed enzyme, whereas for EG II the corresponding curve leveled off at both 4 and 40 degrees C. At low conversion, below 1%, EG II produced as much soluble sugars as CBH I. At higher conversion, CBH I was more efficient than EG II. The synergism as function of adsorbed enzyme increased with bound enzyme before reaching a stable value of about 2. The effect of varying the ratio of CBH I:EG II was studied at fixed total enzyme loading and by changing the ratio between the enzymes. Only a small addition (5%) of EG II to a CBH I solution was shown to be sufficient for nearly maximal synergism. The ratio between EG II and CBH I was not critical. The ratio 40% EG II:60% CBH I showed similar conversion to 5% EG II:95% CBH I. Modifications of the conventional endo-exo synergism model are proposed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Karlsson</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Center for Chemistry and Chemical Engineering, Lund University, PO Box 124, S-221 00 Lund, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Medve</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Tjerneld</LastName><ForeName>F</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Biochem Biotechnol</MedlineTA><NlmUniqueID>8208561</NlmUniqueID><ISSNLinking>0273-2289</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>1998</Year><Month>12</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>1999</Year><Month>06</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>1999</Year><Month>07</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>8</Month><Day>12</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>8</Month><Day>12</Day><Hour>5</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>8</Month><Day>12</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15304773</ArticleId><ArticleId IdType="pii">ABAB:82:3:243</ArticleId><ArticleId IdType="doi">10.1385/abab:82:3:243</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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