New pulp biobleaching system involving manganese peroxidase immobilized in a silica support with controlled pore sizes.
Identifieur interne : 000A34 ( Main/Exploration ); précédent : 000A33; suivant : 000A35New pulp biobleaching system involving manganese peroxidase immobilized in a silica support with controlled pore sizes.
Auteurs : T. Sasaki [Japon] ; T. Kajino ; B. Li ; H. Sugiyama ; H. TakahashiSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 2001.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Silice.
- enzymologie : Phanerochaete.
- métabolisme : Enzymes immobilisées, Peroxidases.
- Bois, Gel de silice, Peroxyde d'hydrogène, Stabilité enzymatique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Silicon Dioxide.
- chemical , metabolism : Enzymes, Immobilized, Peroxidases.
- enzymology : Phanerochaete.
- Enzyme Stability, Hydrogen Peroxide, Silica Gel, Wood.
Abstract
Attempts have been made to use manganese peroxidase (MnP) for chlorine-free pulp biobleaching, but they have not been commercially viable because of the enzyme's low stability. We developed a new pulp biobleaching method involving mesoporous material-immobilized manganese peroxidase from Phanerochaete chrysosporium. MnP immobilized in FSM-16, a folded-sheet mesoporous material whose pore size is nearly the same as the diameter of the enzyme, had the highest thermal stability and tolerance to H(2)O(2). MnP immobilized in FSM-16 retained more than 80% of its initial activity even after 10 days of continuous reaction. We constructed a thermally discontinuous two-stage reactor system, in which the enzyme (39 degrees C) and pulp-bleaching (70 degrees C) reactions were performed separately. When the treatment of pulp with MnP by means of the two-stage reactor system and alkaline extraction was repeated seven times, the brightness of the pulp increased to about 88% within 7 h after completion of the last treatment.
DOI: 10.1128/AEM.67.5.2208-2212.2001
PubMed: 11319102
PubMed Central: PMC92857
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Li</name></author><author><name sortKey="Sugiyama, H" sort="Sugiyama, H" uniqKey="Sugiyama H" first="H" last="Sugiyama">H. Sugiyama</name></author><author><name sortKey="Takahashi, H" sort="Takahashi, H" uniqKey="Takahashi H" first="H" last="Takahashi">H. 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We developed a new pulp biobleaching method involving mesoporous material-immobilized manganese peroxidase from Phanerochaete chrysosporium. MnP immobilized in FSM-16, a folded-sheet mesoporous material whose pore size is nearly the same as the diameter of the enzyme, had the highest thermal stability and tolerance to H(2)O(2). MnP immobilized in FSM-16 retained more than 80% of its initial activity even after 10 days of continuous reaction. We constructed a thermally discontinuous two-stage reactor system, in which the enzyme (39 degrees C) and pulp-bleaching (70 degrees C) reactions were performed separately. When the treatment of pulp with MnP by means of the two-stage reactor system and alkaline extraction was repeated seven times, the brightness of the pulp increased to about 88% within 7 h after completion of the last treatment.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11319102</PMID><DateCompleted><Year>2001</Year><Month>09</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0099-2240</ISSN><JournalIssue CitedMedium="Print"><Volume>67</Volume><Issue>5</Issue><PubDate><Year>2001</Year><Month>May</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>New pulp biobleaching system involving manganese peroxidase immobilized in a silica support with controlled pore sizes.</ArticleTitle><Pagination><MedlinePgn>2208-12</MedlinePgn></Pagination><Abstract><AbstractText>Attempts have been made to use manganese peroxidase (MnP) for chlorine-free pulp biobleaching, but they have not been commercially viable because of the enzyme's low stability. We developed a new pulp biobleaching method involving mesoporous material-immobilized manganese peroxidase from Phanerochaete chrysosporium. MnP immobilized in FSM-16, a folded-sheet mesoporous material whose pore size is nearly the same as the diameter of the enzyme, had the highest thermal stability and tolerance to H(2)O(2). MnP immobilized in FSM-16 retained more than 80% of its initial activity even after 10 days of continuous reaction. We constructed a thermally discontinuous two-stage reactor system, in which the enzyme (39 degrees C) and pulp-bleaching (70 degrees C) reactions were performed separately. When the treatment of pulp with MnP by means of the two-stage reactor system and alkaline extraction was repeated seven times, the brightness of the pulp increased to about 88% within 7 h after completion of the last treatment.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sasaki</LastName><ForeName>T</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Toyota Central R&D Laboratories, Inc., 41-1, Yokomichi, Nagakute, Aichi 480-1192, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kajino</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Sugiyama</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author 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IdType="doi">10.1128/AEM.67.5.2208-2212.2001</ArticleId><ArticleId IdType="pmc">PMC92857</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Eur J Biochem. 2000 Jul;267(13):4222-31</Citation><ArticleIdList><ArticleId IdType="pubmed">10866827</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Biochem Biotechnol. 1996 Jul;60(1):1-17</Citation><ArticleIdList><ArticleId IdType="pubmed">8756612</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1991 Jul;288(1):145-8</Citation><ArticleIdList><ArticleId IdType="pubmed">1898012</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1989 Apr;270(1):404-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2930198</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1994 Mar;60(3):921-6</Citation><ArticleIdList><ArticleId IdType="pubmed">16349219</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1994 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IdType="pubmed">10099422</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Kajino, T" sort="Kajino, T" uniqKey="Kajino T" first="T" last="Kajino">T. Kajino</name><name sortKey="Li, B" sort="Li, B" uniqKey="Li B" first="B" last="Li">B. Li</name><name sortKey="Sugiyama, H" sort="Sugiyama, H" uniqKey="Sugiyama H" first="H" last="Sugiyama">H. Sugiyama</name><name sortKey="Takahashi, H" sort="Takahashi, H" uniqKey="Takahashi H" first="H" last="Takahashi">H. Takahashi</name></noCountry><country name="Japon"><noRegion><name sortKey="Sasaki, T" sort="Sasaki, T" uniqKey="Sasaki T" first="T" last="Sasaki">T. Sasaki</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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