Synthesis of enzymes connected with mycoparasitism by ectomycorrhizal fungi.
Identifieur interne : 003370 ( Main/Corpus ); précédent : 003369; suivant : 003371Synthesis of enzymes connected with mycoparasitism by ectomycorrhizal fungi.
Auteurs : Joanna Mucha ; Hanna Dahm ; Edmund Strzelczyk ; Antoni WernerSource :
- Archives of microbiology [ 0302-8933 ] ; 2006.
English descriptors
- KwdEn :
- Animals (MeSH), Chitinases (biosynthesis), Chitinases (metabolism), Glucan 1,3-beta-Glucosidase (biosynthesis), Glucan 1,3-beta-Glucosidase (metabolism), Mycelium (enzymology), Mycelium (metabolism), Mycorrhizae (enzymology), Mycorrhizae (growth & development), Mycorrhizae (metabolism), beta-Glucans (metabolism), beta-Glucosidase (biosynthesis).
- MESH :
- chemical , biosynthesis : Chitinases, Glucan 1,3-beta-Glucosidase, beta-Glucosidase.
- chemical , metabolism : Chitinases, Glucan 1,3-beta-Glucosidase, beta-Glucans.
- enzymology : Mycelium, Mycorrhizae.
- growth & development : Mycorrhizae.
- metabolism : Mycelium, Mycorrhizae.
- Animals.
Abstract
The production of enzymes involved in mycoparasitism by several strains of ectomycorrhizal fungi: Amanita muscaria (16-3), Laccaria laccata (9-12), L. laccata (9-1), Suillus bovinus (15-4), S. bovinus (15-3), S. luteus (14-7) on different substrates such as colloidal chitin, mycelia of Trichoderma harzianum, T. virens and Mucor hiemalis was examined. Chitinases and beta-1,3-glucanases were assayed spectrophotometrically by measuring the amount of reducing sugars releasing from suitable substrate by means of Miller's method. Beta-glucosidases were determined by measuring the amount of p-nitrophenol released from p-nitrophenyl-beta-D-glucopyranoside. It was observed that A. muscaria (16-3) and L. laccata (9-12) biosynthesized the highest activity of enzymes in contrast to the strains of S. bovinus and S. luteus. The mycelium of T. harzianum turned out to be the best substrate for the induction of beta-1,3-glucanases and beta-glucosidases for both strains of L. laccata, although the difference in the induction of chitinases in the presence of mycelia of different species of Trichoderma was not indicated.
DOI: 10.1007/s00203-005-0068-2
PubMed: 16395555
Links to Exploration step
pubmed:16395555Le document en format XML
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Chitinases and beta-1,3-glucanases were assayed spectrophotometrically by measuring the amount of reducing sugars releasing from suitable substrate by means of Miller's method. Beta-glucosidases were determined by measuring the amount of p-nitrophenol released from p-nitrophenyl-beta-D-glucopyranoside. It was observed that A. muscaria (16-3) and L. laccata (9-12) biosynthesized the highest activity of enzymes in contrast to the strains of S. bovinus and S. luteus. The mycelium of T. harzianum turned out to be the best substrate for the induction of beta-1,3-glucanases and beta-glucosidases for both strains of L. laccata, although the difference in the induction of chitinases in the presence of mycelia of different species of Trichoderma was not indicated.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16395555</PMID><DateCompleted><Year>2007</Year><Month>08</Month><Day>03</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0302-8933</ISSN><JournalIssue CitedMedium="Print"><Volume>185</Volume><Issue>1</Issue><PubDate><Year>2006</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Archives of microbiology</Title><ISOAbbreviation>Arch Microbiol</ISOAbbreviation></Journal><ArticleTitle>Synthesis of enzymes connected with mycoparasitism by ectomycorrhizal fungi.</ArticleTitle><Pagination><MedlinePgn>69-77</MedlinePgn></Pagination><Abstract><AbstractText>The production of enzymes involved in mycoparasitism by several strains of ectomycorrhizal fungi: Amanita muscaria (16-3), Laccaria laccata (9-12), L. laccata (9-1), Suillus bovinus (15-4), S. bovinus (15-3), S. luteus (14-7) on different substrates such as colloidal chitin, mycelia of Trichoderma harzianum, T. virens and Mucor hiemalis was examined. Chitinases and beta-1,3-glucanases were assayed spectrophotometrically by measuring the amount of reducing sugars releasing from suitable substrate by means of Miller's method. Beta-glucosidases were determined by measuring the amount of p-nitrophenol released from p-nitrophenyl-beta-D-glucopyranoside. It was observed that A. muscaria (16-3) and L. laccata (9-12) biosynthesized the highest activity of enzymes in contrast to the strains of S. bovinus and S. luteus. The mycelium of T. harzianum turned out to be the best substrate for the induction of beta-1,3-glucanases and beta-glucosidases for both strains of L. laccata, although the difference in the induction of chitinases in the presence of mycelia of different species of Trichoderma was not indicated.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mucha</LastName><ForeName>Joanna</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Laboratory of Root Pathology, Institute of Dendrology, Polish Academy of Sciences, Parkowa 5, 62-035, Kórnik, Poland. mucha_joanna@wp.pl</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dahm</LastName><ForeName>Hanna</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Strzelczyk</LastName><ForeName>Edmund</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Werner</LastName><ForeName>Antoni</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>01</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Arch Microbiol</MedlineTA><NlmUniqueID>0410427</NlmUniqueID><ISSNLinking>0302-8933</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047071">beta-Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>9051-97-2</RegistryNumber><NameOfSubstance UI="C033363">beta-1,3-glucan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.14</RegistryNumber><NameOfSubstance UI="D002688">Chitinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber><NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.58</RegistryNumber><NameOfSubstance UI="D043326">Glucan 1,3-beta-Glucosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002688" MajorTopicYN="N">Chitinases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043326" MajorTopicYN="N">Glucan 1,3-beta-Glucosidase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D025282" MajorTopicYN="N">Mycelium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D038821" MajorTopicYN="N">Mycorrhizae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D047071" MajorTopicYN="N">beta-Glucans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2005</Year><Month>08</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2005</Year><Month>11</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2005</Year><Month>10</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>1</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>8</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>1</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16395555</ArticleId><ArticleId IdType="doi">10.1007/s00203-005-0068-2</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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