Influence of Veratryl Alcohol and Hydrogen Peroxide on Ligninase Activity and Ligninase Production by Phanerochaete chrysosporium.
Identifieur interne : 001011 ( Main/Exploration ); précédent : 001010; suivant : 001012Influence of Veratryl Alcohol and Hydrogen Peroxide on Ligninase Activity and Ligninase Production by Phanerochaete chrysosporium.
Auteurs : F. Tonon [France] ; E. OdierSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1988.
Abstract
Veratryl alcohol, added as a supplement to cultures of Phanerochaete chrysosporium, enhanced ligninase activity through protection of the ligninase against inactivation by hydrogen peroxide produced by this fungus in cultures. In the presence of veratryl alcohol, the loss of ligninase activity observed in non-protein-synthesizing cultures (cycloheximide-treated) equaled the extracellular protein turnover. When cultures were not supplemented with veratryl alcohol, inactivation of ligninase by hydrogen peroxide added to protein turnover, resulting in a more rapid loss of ligninase activity. Although all ligninase isoenzymes are sensitive to inactivation by hydrogen peroxide, only the isoenzyme of the highest specific activity (80.6 nkat . mg of protein; M(r), 41,800; pI, 3.96) was found to be protected by veratryl alcohol. The concentration of veratryl alcohol necessary for full protection of ligninase activity varied according to the concentration of hydrogen peroxide present in the medium, which depended on the nature of the carbon source (glucose or glycerol). It is proposed that the nature of the carbon source influences the overall ligninase activity not only directly, by affecting the rate and the type of synthesized ligninase, but also by affecting the rate of hydrogen peroxide production, bringing about different rates of inactivation.
DOI: 10.1128/AEM.54.2.466-472.1988
PubMed: 16347560
PubMed Central: PMC202474
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Influence of Veratryl Alcohol and Hydrogen Peroxide on Ligninase Activity and Ligninase Production by Phanerochaete chrysosporium.</title><author><name sortKey="Tonon, F" sort="Tonon, F" uniqKey="Tonon F" first="F" last="Tonon">F. Tonon</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire de Microbiologie, Centre de Biotechnologies Agro-Industrielles, Institut National de la Recherche Agronomique, 78850 Thiverval-Grignon, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Microbiologie, Centre de Biotechnologies Agro-Industrielles, Institut National de la Recherche Agronomique, 78850 Thiverval-Grignon</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Thiverval-Grignon</settlement></placeName></affiliation></author><author><name sortKey="Odier, E" sort="Odier, E" uniqKey="Odier E" first="E" last="Odier">E. Odier</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1988">1988</date><idno type="RBID">pubmed:16347560</idno><idno type="pmid">16347560</idno><idno type="pmc">PMC202474</idno><idno type="doi">10.1128/AEM.54.2.466-472.1988</idno><idno type="wicri:Area/Main/Corpus">001013</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001013</idno><idno type="wicri:Area/Main/Curation">001013</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001013</idno><idno type="wicri:Area/Main/Exploration">001013</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Influence of Veratryl Alcohol and Hydrogen Peroxide on Ligninase Activity and Ligninase Production by Phanerochaete chrysosporium.</title><author><name sortKey="Tonon, F" sort="Tonon, F" uniqKey="Tonon F" first="F" last="Tonon">F. Tonon</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire de Microbiologie, Centre de Biotechnologies Agro-Industrielles, Institut National de la Recherche Agronomique, 78850 Thiverval-Grignon, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Microbiologie, Centre de Biotechnologies Agro-Industrielles, Institut National de la Recherche Agronomique, 78850 Thiverval-Grignon</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Thiverval-Grignon</settlement></placeName></affiliation></author><author><name sortKey="Odier, E" sort="Odier, E" uniqKey="Odier E" first="E" last="Odier">E. Odier</name></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno type="ISSN">0099-2240</idno><imprint><date when="1988" type="published">1988</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Veratryl alcohol, added as a supplement to cultures of Phanerochaete chrysosporium, enhanced ligninase activity through protection of the ligninase against inactivation by hydrogen peroxide produced by this fungus in cultures. In the presence of veratryl alcohol, the loss of ligninase activity observed in non-protein-synthesizing cultures (cycloheximide-treated) equaled the extracellular protein turnover. When cultures were not supplemented with veratryl alcohol, inactivation of ligninase by hydrogen peroxide added to protein turnover, resulting in a more rapid loss of ligninase activity. Although all ligninase isoenzymes are sensitive to inactivation by hydrogen peroxide, only the isoenzyme of the highest specific activity (80.6 nkat . mg of protein; M(r), 41,800; pI, 3.96) was found to be protected by veratryl alcohol. The concentration of veratryl alcohol necessary for full protection of ligninase activity varied according to the concentration of hydrogen peroxide present in the medium, which depended on the nature of the carbon source (glucose or glycerol). It is proposed that the nature of the carbon source influences the overall ligninase activity not only directly, by affecting the rate and the type of synthesized ligninase, but also by affecting the rate of hydrogen peroxide production, bringing about different rates of inactivation.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">16347560</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>27</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0099-2240</ISSN><JournalIssue CitedMedium="Print"><Volume>54</Volume><Issue>2</Issue><PubDate><Year>1988</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Influence of Veratryl Alcohol and Hydrogen Peroxide on Ligninase Activity and Ligninase Production by Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>466-72</MedlinePgn></Pagination><Abstract><AbstractText>Veratryl alcohol, added as a supplement to cultures of Phanerochaete chrysosporium, enhanced ligninase activity through protection of the ligninase against inactivation by hydrogen peroxide produced by this fungus in cultures. In the presence of veratryl alcohol, the loss of ligninase activity observed in non-protein-synthesizing cultures (cycloheximide-treated) equaled the extracellular protein turnover. When cultures were not supplemented with veratryl alcohol, inactivation of ligninase by hydrogen peroxide added to protein turnover, resulting in a more rapid loss of ligninase activity. Although all ligninase isoenzymes are sensitive to inactivation by hydrogen peroxide, only the isoenzyme of the highest specific activity (80.6 nkat . mg of protein; M(r), 41,800; pI, 3.96) was found to be protected by veratryl alcohol. The concentration of veratryl alcohol necessary for full protection of ligninase activity varied according to the concentration of hydrogen peroxide present in the medium, which depended on the nature of the carbon source (glucose or glycerol). It is proposed that the nature of the carbon source influences the overall ligninase activity not only directly, by affecting the rate and the type of synthesized ligninase, but also by affecting the rate of hydrogen peroxide production, bringing about different rates of inactivation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tonon</LastName><ForeName>F</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Laboratoire de Microbiologie, Centre de Biotechnologies Agro-Industrielles, Institut National de la Recherche Agronomique, 78850 Thiverval-Grignon, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Odier</LastName><ForeName>E</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Environ Microbiol</MedlineTA><NlmUniqueID>7605801</NlmUniqueID><ISSNLinking>0099-2240</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1988</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1988</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1988</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16347560</ArticleId><ArticleId IdType="pmc">PMC202474</ArticleId><ArticleId IdType="doi">10.1128/AEM.54.2.466-472.1988</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Bacteriol. 1978 Sep;135(3):790-7</Citation><ArticleIdList><ArticleId IdType="pubmed">690075</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1976 May 7;72:248-54</Citation><ArticleIdList><ArticleId IdType="pubmed">942051</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1985 Mar 10;260(5):2609-12</Citation><ArticleIdList><ArticleId IdType="pubmed">2982828</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1987 May;169(5):2195-201</Citation><ArticleIdList><ArticleId IdType="pubmed">3553159</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1986 May 25;261(15):6900-3</Citation><ArticleIdList><ArticleId IdType="pubmed">3700421</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1985 Aug 15;241(1):304-14</Citation><ArticleIdList><ArticleId IdType="pubmed">4026322</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1983 Aug 12;221(4611):661-3</Citation><ArticleIdList><ArticleId IdType="pubmed">17787736</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1982 Sep;44(3):732-6</Citation><ArticleIdList><ArticleId IdType="pubmed">16346099</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1983 Nov;46(5):1140-5</Citation><ArticleIdList><ArticleId IdType="pubmed">16346420</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1985 Feb;49(2):299-304</Citation><ArticleIdList><ArticleId IdType="pubmed">16346716</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1986 Aug;52(2):251-4</Citation><ArticleIdList><ArticleId IdType="pubmed">16347125</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1984 Apr;81(8):2280-4</Citation><ArticleIdList><ArticleId IdType="pubmed">16593451</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 1983 Aug 12;114(3):1077-83</Citation><ArticleIdList><ArticleId IdType="pubmed">6615503</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Thiverval-Grignon</li></settlement></list><tree><noCountry><name sortKey="Odier, E" sort="Odier, E" uniqKey="Odier E" first="E" last="Odier">E. Odier</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Tonon, F" sort="Tonon, F" uniqKey="Tonon F" first="F" last="Tonon">F. Tonon</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001011 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001011 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:16347560
|texte= Influence of Veratryl Alcohol and Hydrogen Peroxide on Ligninase Activity and Ligninase Production by Phanerochaete chrysosporium.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:16347560" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |