Comparison of different fungal enzymes for bleaching high-quality paper pulps.
Identifieur interne : 000847 ( Main/Exploration ); précédent : 000846; suivant : 000848Comparison of different fungal enzymes for bleaching high-quality paper pulps.
Auteurs : Cécile Sigoillot [France] ; Susana Camarero ; Teresa Vidal ; Eric Record ; Michèle Asther ; Marta Pérez-Boada ; María Jesús Martínez ; Jean-Claude Sigoillot ; Marcel Asther ; José F. Colom ; Angel T. MartínezSource :
- Journal of biotechnology [ 0168-1656 ] ; 2005.
Descripteurs français
- KwdFr :
- Aspergillus niger (enzymologie), Aspergillus niger (génétique), Biotechnologie (méthodes), Concentration en ions d'hydrogène (MeSH), Hydrolases (métabolisme), Laccase (métabolisme), Lignine (métabolisme), Microbiologie industrielle (MeSH), Oxidoreductases (métabolisme), Papier (MeSH), Phanerochaete (enzymologie), Phanerochaete (génétique), Pleurotus (enzymologie), Pleurotus (génétique), Protéines recombinantes (métabolisme), Triazoles (métabolisme).
- MESH :
- enzymologie : Aspergillus niger, Phanerochaete, Pleurotus.
- génétique : Aspergillus niger, Phanerochaete, Pleurotus.
- métabolisme : Hydrolases, Laccase, Lignine, Oxidoreductases, Protéines recombinantes, Triazoles.
- méthodes : Biotechnologie.
- Concentration en ions d'hydrogène, Microbiologie industrielle, Papier.
English descriptors
- KwdEn :
- Aspergillus niger (enzymology), Aspergillus niger (genetics), Biotechnology (methods), Hydrogen-Ion Concentration (MeSH), Hydrolases (metabolism), Industrial Microbiology (MeSH), Laccase (metabolism), Lignin (metabolism), Oxidoreductases (metabolism), Paper (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Pleurotus (enzymology), Pleurotus (genetics), Recombinant Proteins (metabolism), Triazoles (metabolism).
- MESH :
- chemical , metabolism : Hydrolases, Laccase, Lignin, Oxidoreductases, Recombinant Proteins, Triazoles.
- enzymology : Aspergillus niger, Phanerochaete, Pleurotus.
- genetics : Aspergillus niger, Phanerochaete, Pleurotus.
- methods : Biotechnology.
- Hydrogen-Ion Concentration, Industrial Microbiology, Paper.
Abstract
Wild and recombinant hydrolases and oxidoreductases with a potential interest for environmentally sound bleaching of high-quality paper pulp (from flax) were incorporated into a totally chlorine free (TCF) sequence that also included a peroxide stage. The ability of feruloyl esterase (from Aspergillus niger) and Mn2+-oxidizing peroxidases (from Phanerochaete chrysosporium and Pleurotus eryngii) to decrease the final lignin content of flax pulp was shown. Laccase from Pycnoporus cinnabarinus (without mediator) also caused a slight improvement of pulp brightness that was increased in the presence of aryl-alcohol oxidase. However, the best results were obtained when the laccase treatment was performed in the presence of a mediator, 1-hydroxybenzotriazol (HBT), enabling strong delignification of pulps. The enzymatic removal of lignin resulted in high-final brightness values that are difficult to attain by chemical bleaching of this type of pulp. A partial inactivation of laccase by HBT was observed but this negative effect was strongly reduced in the presence of pulp. The good results obtained with the same laccase expressed in A. niger at bioreactor scale, revealed the feasibility of using recombinant laccase for bleaching high-quality non-wood pulps in the presence of a mediator.
DOI: 10.1016/j.jbiotec.2004.09.006
PubMed: 15639095
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Colom</name></author><author><name sortKey="Martinez, Angel T" sort="Martinez, Angel T" uniqKey="Martinez A" first="Angel T" last="Martínez">Angel T. Martínez</name></author></analytic><series><title level="j">Journal of biotechnology</title><idno type="ISSN">0168-1656</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aspergillus niger (enzymology)</term><term>Aspergillus niger (genetics)</term><term>Biotechnology (methods)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Hydrolases (metabolism)</term><term>Industrial Microbiology (MeSH)</term><term>Laccase (metabolism)</term><term>Lignin (metabolism)</term><term>Oxidoreductases (metabolism)</term><term>Paper (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Pleurotus (enzymology)</term><term>Pleurotus (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Triazoles (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aspergillus niger (enzymologie)</term><term>Aspergillus niger (génétique)</term><term>Biotechnologie (méthodes)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Hydrolases (métabolisme)</term><term>Laccase (métabolisme)</term><term>Lignine (métabolisme)</term><term>Microbiologie industrielle (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Papier (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Pleurotus (enzymologie)</term><term>Pleurotus (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Triazoles (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hydrolases</term><term>Laccase</term><term>Lignin</term><term>Oxidoreductases</term><term>Recombinant Proteins</term><term>Triazoles</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Aspergillus niger</term><term>Phanerochaete</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Aspergillus niger</term><term>Phanerochaete</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Aspergillus niger</term><term>Phanerochaete</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Aspergillus niger</term><term>Phanerochaete</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Biotechnology</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Hydrolases</term><term>Laccase</term><term>Lignine</term><term>Oxidoreductases</term><term>Protéines recombinantes</term><term>Triazoles</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Biotechnologie</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Industrial Microbiology</term><term>Paper</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Microbiologie industrielle</term><term>Papier</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Wild and recombinant hydrolases and oxidoreductases with a potential interest for environmentally sound bleaching of high-quality paper pulp (from flax) were incorporated into a totally chlorine free (TCF) sequence that also included a peroxide stage. The ability of feruloyl esterase (from Aspergillus niger) and Mn2+-oxidizing peroxidases (from Phanerochaete chrysosporium and Pleurotus eryngii) to decrease the final lignin content of flax pulp was shown. Laccase from Pycnoporus cinnabarinus (without mediator) also caused a slight improvement of pulp brightness that was increased in the presence of aryl-alcohol oxidase. However, the best results were obtained when the laccase treatment was performed in the presence of a mediator, 1-hydroxybenzotriazol (HBT), enabling strong delignification of pulps. The enzymatic removal of lignin resulted in high-final brightness values that are difficult to attain by chemical bleaching of this type of pulp. A partial inactivation of laccase by HBT was observed but this negative effect was strongly reduced in the presence of pulp. The good results obtained with the same laccase expressed in A. niger at bioreactor scale, revealed the feasibility of using recombinant laccase for bleaching high-quality non-wood pulps in the presence of a mediator.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15639095</PMID><DateCompleted><Year>2005</Year><Month>05</Month><Day>19</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0168-1656</ISSN><JournalIssue CitedMedium="Print"><Volume>115</Volume><Issue>4</Issue><PubDate><Year>2005</Year><Month>Feb</Month><Day>23</Day></PubDate></JournalIssue><Title>Journal of biotechnology</Title><ISOAbbreviation>J Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Comparison of different fungal enzymes for bleaching high-quality paper pulps.</ArticleTitle><Pagination><MedlinePgn>333-43</MedlinePgn></Pagination><Abstract><AbstractText>Wild and recombinant hydrolases and oxidoreductases with a potential interest for environmentally sound bleaching of high-quality paper pulp (from flax) were incorporated into a totally chlorine free (TCF) sequence that also included a peroxide stage. The ability of feruloyl esterase (from Aspergillus niger) and Mn2+-oxidizing peroxidases (from Phanerochaete chrysosporium and Pleurotus eryngii) to decrease the final lignin content of flax pulp was shown. Laccase from Pycnoporus cinnabarinus (without mediator) also caused a slight improvement of pulp brightness that was increased in the presence of aryl-alcohol oxidase. However, the best results were obtained when the laccase treatment was performed in the presence of a mediator, 1-hydroxybenzotriazol (HBT), enabling strong delignification of pulps. The enzymatic removal of lignin resulted in high-final brightness values that are difficult to attain by chemical bleaching of this type of pulp. A partial inactivation of laccase by HBT was observed but this negative effect was strongly reduced in the presence of pulp. The good results obtained with the same laccase expressed in A. niger at bioreactor scale, revealed the feasibility of using recombinant laccase for bleaching high-quality non-wood pulps in the presence of a mediator.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sigoillot</LastName><ForeName>Cécile</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>UMR 1163 INRA/UP UBCF, CP 925, 163 Avenue Luminy, F-13288 Marseille Cedex 09, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Camarero</LastName><ForeName>Susana</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Vidal</LastName><ForeName>Teresa</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Record</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Asther</LastName><ForeName>Michèle</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Pérez-Boada</LastName><ForeName>Marta</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>María Jesús</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Sigoillot</LastName><ForeName>Jean-Claude</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Asther</LastName><ForeName>Marcel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Colom</LastName><ForeName>José F</ForeName><Initials>JF</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>Angel T</ForeName><Initials>AT</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2004</Year><Month>11</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Biotechnol</MedlineTA><NlmUniqueID>8411927</NlmUniqueID><ISSNLinking>0168-1656</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014230">Triazoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>A2T929DMG4</RegistryNumber><NameOfSubstance UI="C011852">1-hydroxybenzotriazole</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.-</RegistryNumber><NameOfSubstance UI="D006867">Hydrolases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001234" MajorTopicYN="N">Aspergillus niger</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001709" MajorTopicYN="N">Biotechnology</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006867" MajorTopicYN="N">Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007218" MajorTopicYN="Y">Industrial Microbiology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010209" MajorTopicYN="Y">Paper</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020076" 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PubStatus="pubmed"><Year>2005</Year><Month>1</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>5</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>1</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15639095</ArticleId><ArticleId IdType="pii">S0168-1656(04)00479-1</ArticleId><ArticleId IdType="doi">10.1016/j.jbiotec.2004.09.006</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement></list><tree><noCountry><name sortKey="Asther, Marcel" sort="Asther, Marcel" uniqKey="Asther M" first="Marcel" last="Asther">Marcel Asther</name><name sortKey="Asther, Michele" sort="Asther, Michele" uniqKey="Asther M" first="Michèle" last="Asther">Michèle Asther</name><name sortKey="Camarero, Susana" sort="Camarero, Susana" uniqKey="Camarero S" first="Susana" last="Camarero">Susana Camarero</name><name sortKey="Colom, Jose F" sort="Colom, Jose F" uniqKey="Colom J" first="José F" last="Colom">José F. Colom</name><name sortKey="Martinez, Angel T" sort="Martinez, Angel T" uniqKey="Martinez A" first="Angel T" last="Martínez">Angel T. Martínez</name><name sortKey="Martinez, Maria Jesus" sort="Martinez, Maria Jesus" uniqKey="Martinez M" first="María Jesús" last="Martínez">María Jesús Martínez</name><name sortKey="Perez Boada, Marta" sort="Perez Boada, Marta" uniqKey="Perez Boada M" first="Marta" last="Pérez-Boada">Marta Pérez-Boada</name><name sortKey="Record, Eric" sort="Record, Eric" uniqKey="Record E" first="Eric" last="Record">Eric Record</name><name sortKey="Sigoillot, Jean Claude" sort="Sigoillot, Jean Claude" uniqKey="Sigoillot J" first="Jean-Claude" last="Sigoillot">Jean-Claude Sigoillot</name><name sortKey="Vidal, Teresa" sort="Vidal, Teresa" uniqKey="Vidal T" first="Teresa" last="Vidal">Teresa Vidal</name></noCountry><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Sigoillot, Cecile" sort="Sigoillot, Cecile" uniqKey="Sigoillot C" first="Cécile" last="Sigoillot">Cécile Sigoillot</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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