[Enzyme regeneration during hydrolysis of steam-pretreated willow and requirement for cellulase complex composition].
Identifieur interne : 002071 ( Main/Exploration ); précédent : 002070; suivant : 002072[Enzyme regeneration during hydrolysis of steam-pretreated willow and requirement for cellulase complex composition].
Auteurs : A A Pristavka [Russie] ; V P Salovarova ; Z. Zacchi ; I V Berezin ; M L RabinovichSource :
- Prikladnaia biokhimiia i mikrobiologiia [ 0555-1099 ]
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Aspergillus, Trichoderma.
- métabolisme : Arbres, Cellulase.
- Activation enzymatique, Hydrolyse, Vapeur.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cellulase.
- enzymology : Aspergillus, Trichoderma.
- metabolism : Trees.
- Enzyme Activation, Hydrolysis, Steam.
Abstract
In order to reduce the total enzyme consumption in high-solids static hydrolysis of nonwashed steam-exploded willow Salix caprea by mixed cellulase of Trichoderma reesei + Aspergillus foetidus, two different approaches were proposed. In the first case, the enzyme activity adsorbed on residual solids after extended hydrolysis was used for hydrolysis of the newly added substrate. The initial mixing of fresh and hydrolyzed substrates was sufficient for the adsorbed enzyme redistribution and conversion of the new substrate portion, and permanent mechanical stirring was not required. Feeding of two additional portions of the exploded hardwood adjusted to pH 4 with dry caustic into the reactor with simultaneous replacement of accumulated sugars with fresh buffer (pH 4.5) resulted, on average, in a 90% conversion of cellulose at the final enzyme loading 8 IFPU per g ODM substrate, an average sugar concentration of 12%, and a glucose/xylose ratio of 5:1. In the second approach, weakly adsorbed cellulase fractions were used for static high-solids hydrolysis followed by their ultrafiltration recovery from the resultant sugar syrup. In contrast to the initial cellulase mixture whose residual activity in a syrup did not exceed 5-10% at the end of hydrolysis (48 h), up to 60% of weakly adsorbed enzyme fraction could be separated from sugar syrups by ultrafiltration and then reused. Weakly adsorbed enzymes displayed a hydrolysis efficiency of not less than 80% per IFPU enzyme consumed in extended hydrolysis of pretreated willow as compared to the original enzyme mixture. An electrophoretic study of the weakly adsorbed enzyme fraction identified T. reesei cellobiohydrolase II as the predominant component, whereas clear domination of T. reesei cellobiohydrolase I was found by electrophoresis of proteins tightly bound to hydrolysis residual solids.
PubMed: 10867945
Affiliations:
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Zacchi</name></author><author><name sortKey="Berezin, I V" sort="Berezin, I V" uniqKey="Berezin I" first="I V" last="Berezin">I V Berezin</name></author><author><name sortKey="Rabinovich, M L" sort="Rabinovich, M L" uniqKey="Rabinovich M" first="M L" last="Rabinovich">M L Rabinovich</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000 May-Jun</date><idno type="RBID">pubmed:10867945</idno><idno type="pmid">10867945</idno><idno type="wicri:Area/Main/Corpus">002120</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002120</idno><idno type="wicri:Area/Main/Curation">002120</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002120</idno><idno type="wicri:Area/Main/Exploration">002120</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Enzyme regeneration during hydrolysis of steam-pretreated willow and requirement for cellulase complex composition].</title><author><name sortKey="Pristavka, A A" sort="Pristavka, A A" uniqKey="Pristavka A" first="A A" last="Pristavka">A A Pristavka</name><affiliation wicri:level="3"><nlm:affiliation>Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. inbio@glas.apc.org</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Salovarova, V P" sort="Salovarova, V P" uniqKey="Salovarova V" first="V P" last="Salovarova">V P Salovarova</name></author><author><name sortKey="Zacchi, Z" sort="Zacchi, Z" uniqKey="Zacchi Z" first="Z" last="Zacchi">Z. Zacchi</name></author><author><name sortKey="Berezin, I V" sort="Berezin, I V" uniqKey="Berezin I" first="I V" last="Berezin">I V Berezin</name></author><author><name sortKey="Rabinovich, M L" sort="Rabinovich, M L" uniqKey="Rabinovich M" first="M L" last="Rabinovich">M L Rabinovich</name></author></analytic><series><title level="j">Prikladnaia biokhimiia i mikrobiologiia</title><idno type="ISSN">0555-1099</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aspergillus (enzymology)</term><term>Cellulase (metabolism)</term><term>Enzyme Activation (MeSH)</term><term>Hydrolysis (MeSH)</term><term>Steam (MeSH)</term><term>Trees (metabolism)</term><term>Trichoderma (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term><term>Arbres (métabolisme)</term><term>Aspergillus (enzymologie)</term><term>Cellulase (métabolisme)</term><term>Hydrolyse (MeSH)</term><term>Trichoderma (enzymologie)</term><term>Vapeur (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Aspergillus</term><term>Trichoderma</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Aspergillus</term><term>Trichoderma</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Trees</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arbres</term><term>Cellulase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme Activation</term><term>Hydrolysis</term><term>Steam</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Hydrolyse</term><term>Vapeur</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In order to reduce the total enzyme consumption in high-solids static hydrolysis of nonwashed steam-exploded willow Salix caprea by mixed cellulase of Trichoderma reesei + Aspergillus foetidus, two different approaches were proposed. In the first case, the enzyme activity adsorbed on residual solids after extended hydrolysis was used for hydrolysis of the newly added substrate. The initial mixing of fresh and hydrolyzed substrates was sufficient for the adsorbed enzyme redistribution and conversion of the new substrate portion, and permanent mechanical stirring was not required. Feeding of two additional portions of the exploded hardwood adjusted to pH 4 with dry caustic into the reactor with simultaneous replacement of accumulated sugars with fresh buffer (pH 4.5) resulted, on average, in a 90% conversion of cellulose at the final enzyme loading 8 IFPU per g ODM substrate, an average sugar concentration of 12%, and a glucose/xylose ratio of 5:1. In the second approach, weakly adsorbed cellulase fractions were used for static high-solids hydrolysis followed by their ultrafiltration recovery from the resultant sugar syrup. In contrast to the initial cellulase mixture whose residual activity in a syrup did not exceed 5-10% at the end of hydrolysis (48 h), up to 60% of weakly adsorbed enzyme fraction could be separated from sugar syrups by ultrafiltration and then reused. Weakly adsorbed enzymes displayed a hydrolysis efficiency of not less than 80% per IFPU enzyme consumed in extended hydrolysis of pretreated willow as compared to the original enzyme mixture. An electrophoretic study of the weakly adsorbed enzyme fraction identified T. reesei cellobiohydrolase II as the predominant component, whereas clear domination of T. reesei cellobiohydrolase I was found by electrophoresis of proteins tightly bound to hydrolysis residual solids.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10867945</PMID><DateCompleted><Year>2000</Year><Month>08</Month><Day>08</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0555-1099</ISSN><JournalIssue CitedMedium="Print"><Volume>36</Volume><Issue>3</Issue><PubDate><MedlineDate>2000 May-Jun</MedlineDate></PubDate></JournalIssue><Title>Prikladnaia biokhimiia i mikrobiologiia</Title><ISOAbbreviation>Prikl Biokhim Mikrobiol</ISOAbbreviation></Journal><ArticleTitle>[Enzyme regeneration during hydrolysis of steam-pretreated willow and requirement for cellulase complex composition].</ArticleTitle><Pagination><MedlinePgn>278-86</MedlinePgn></Pagination><Abstract><AbstractText>In order to reduce the total enzyme consumption in high-solids static hydrolysis of nonwashed steam-exploded willow Salix caprea by mixed cellulase of Trichoderma reesei + Aspergillus foetidus, two different approaches were proposed. In the first case, the enzyme activity adsorbed on residual solids after extended hydrolysis was used for hydrolysis of the newly added substrate. The initial mixing of fresh and hydrolyzed substrates was sufficient for the adsorbed enzyme redistribution and conversion of the new substrate portion, and permanent mechanical stirring was not required. Feeding of two additional portions of the exploded hardwood adjusted to pH 4 with dry caustic into the reactor with simultaneous replacement of accumulated sugars with fresh buffer (pH 4.5) resulted, on average, in a 90% conversion of cellulose at the final enzyme loading 8 IFPU per g ODM substrate, an average sugar concentration of 12%, and a glucose/xylose ratio of 5:1. In the second approach, weakly adsorbed cellulase fractions were used for static high-solids hydrolysis followed by their ultrafiltration recovery from the resultant sugar syrup. In contrast to the initial cellulase mixture whose residual activity in a syrup did not exceed 5-10% at the end of hydrolysis (48 h), up to 60% of weakly adsorbed enzyme fraction could be separated from sugar syrups by ultrafiltration and then reused. Weakly adsorbed enzymes displayed a hydrolysis efficiency of not less than 80% per IFPU enzyme consumed in extended hydrolysis of pretreated willow as compared to the original enzyme mixture. An electrophoretic study of the weakly adsorbed enzyme fraction identified T. reesei cellobiohydrolase II as the predominant component, whereas clear domination of T. reesei cellobiohydrolase I was found by electrophoresis of proteins tightly bound to hydrolysis residual solids.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pristavka</LastName><ForeName>A A</ForeName><Initials>AA</Initials><AffiliationInfo><Affiliation>Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. inbio@glas.apc.org</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Salovarova</LastName><ForeName>V P</ForeName><Initials>VP</Initials></Author><Author ValidYN="Y"><LastName>Zacchi</LastName><ForeName>Z</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Berezin</LastName><ForeName>I V</ForeName><Initials>IV</Initials></Author><Author ValidYN="Y"><LastName>Rabinovich</LastName><ForeName>M L</ForeName><Initials>ML</Initials></Author></AuthorList><Language>rus</Language><PublicationTypeList><PublicationType UI="D004740">English Abstract</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><VernacularTitle>Regeneratsiia fermenta pri gidrolize predobrabotannoĭ parovmy vzyvom drevesiny ivy i trebovaniia k sostavu tselliulaznogo kompleksa.</VernacularTitle></Article><MedlineJournalInfo><Country>Russia (Federation)</Country><MedlineTA>Prikl Biokhim Mikrobiol</MedlineTA><NlmUniqueID>0023416</NlmUniqueID><ISSNLinking>0555-1099</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013227">Steam</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001230" MajorTopicYN="N">Aspergillus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013227" MajorTopicYN="N">Steam</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014242" MajorTopicYN="N">Trichoderma</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>6</Month><Day>27</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>8</Month><Day>12</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>6</Month><Day>27</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10867945</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><noCountry><name sortKey="Berezin, I V" sort="Berezin, I V" uniqKey="Berezin I" first="I V" last="Berezin">I V Berezin</name><name sortKey="Rabinovich, M L" sort="Rabinovich, M L" uniqKey="Rabinovich M" first="M L" last="Rabinovich">M L Rabinovich</name><name sortKey="Salovarova, V P" sort="Salovarova, V P" uniqKey="Salovarova V" first="V P" last="Salovarova">V P Salovarova</name><name sortKey="Zacchi, Z" sort="Zacchi, Z" uniqKey="Zacchi Z" first="Z" last="Zacchi">Z. Zacchi</name></noCountry><country name="Russie"><region name="District fédéral central"><name sortKey="Pristavka, A A" sort="Pristavka, A A" uniqKey="Pristavka A" first="A A" last="Pristavka">A A Pristavka</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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