Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut

Detalhes bibliográficos
Autor(a) principal: Gajera,H. P.
Data de Publicação: 2012
Outros Autores: Vakharia,D. N
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Microbiology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000100005
Resumo: Twelve isolates of Trichoderma (six of T. harzianum, five of T. viride, one of T. virens), which reduced variably the incidence of collar rot disease caused in peanut by Aspergillus niger Van Tieghem, were evaluated for their potential to produce lytic enzymes during in vitro antagonism. T. viride 60 inhibited highest (86.2%) growth of test fungus followed by T. harzianum 2J (80.4%) at 6 days after inoculation (DAI) on PDA media. The specific activities of chitinase, β-1,3-glucanase and protease were 11, 3.46 and 9 folds higher in T6 antagonist (T. viride 60 and A. niger interactions) followed by 8.72, 2.85 and 9 folds in T8 antagonist (T. harzianum 2J and A. niger interactions), respectively, compared to the activity produced by control petri plate T13 (A. niger alone) at 6 DAI. Activity of these lytic enzymes induced in antagonists' plates comprises the growth of Trichoderma isolates. However, cellulase and poly galacturonase were found least amount in these antagonists treatment. A significant positive correlation (p=0.01) between percentage growth inhibition of test fungus and lytic enzymes - (chitinase, β-1,3-glucanase and protease) in the culture medium of antagonist treatment established a relationship to inhibit growth of fungal pathogen by increasing the levels of these enzymes. Among the Trichoderma isolates, T. viride 60 was found best strain to be used in biological control of plant pathogen A. niger.
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spelling Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanutTrichoderma isolatesAspergillus nigerLytic enzymesAntagonistic interactionTwelve isolates of Trichoderma (six of T. harzianum, five of T. viride, one of T. virens), which reduced variably the incidence of collar rot disease caused in peanut by Aspergillus niger Van Tieghem, were evaluated for their potential to produce lytic enzymes during in vitro antagonism. T. viride 60 inhibited highest (86.2%) growth of test fungus followed by T. harzianum 2J (80.4%) at 6 days after inoculation (DAI) on PDA media. The specific activities of chitinase, β-1,3-glucanase and protease were 11, 3.46 and 9 folds higher in T6 antagonist (T. viride 60 and A. niger interactions) followed by 8.72, 2.85 and 9 folds in T8 antagonist (T. harzianum 2J and A. niger interactions), respectively, compared to the activity produced by control petri plate T13 (A. niger alone) at 6 DAI. Activity of these lytic enzymes induced in antagonists' plates comprises the growth of Trichoderma isolates. However, cellulase and poly galacturonase were found least amount in these antagonists treatment. A significant positive correlation (p=0.01) between percentage growth inhibition of test fungus and lytic enzymes - (chitinase, β-1,3-glucanase and protease) in the culture medium of antagonist treatment established a relationship to inhibit growth of fungal pathogen by increasing the levels of these enzymes. Among the Trichoderma isolates, T. viride 60 was found best strain to be used in biological control of plant pathogen A. niger.Sociedade Brasileira de Microbiologia2012-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000100005Brazilian Journal of Microbiology v.43 n.1 2012reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822012000100005info:eu-repo/semantics/openAccessGajera,H. P.Vakharia,D. Neng2012-05-02T00:00:00Zoai:scielo:S1517-83822012000100005Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2012-05-02T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false
dc.title.none.fl_str_mv Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
title Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
spellingShingle Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
Gajera,H. P.
Trichoderma isolates
Aspergillus niger
Lytic enzymes
Antagonistic interaction
title_short Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
title_full Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
title_fullStr Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
title_full_unstemmed Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
title_sort Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut
author Gajera,H. P.
author_facet Gajera,H. P.
Vakharia,D. N
author_role author
author2 Vakharia,D. N
author2_role author
dc.contributor.author.fl_str_mv Gajera,H. P.
Vakharia,D. N
dc.subject.por.fl_str_mv Trichoderma isolates
Aspergillus niger
Lytic enzymes
Antagonistic interaction
topic Trichoderma isolates
Aspergillus niger
Lytic enzymes
Antagonistic interaction
description Twelve isolates of Trichoderma (six of T. harzianum, five of T. viride, one of T. virens), which reduced variably the incidence of collar rot disease caused in peanut by Aspergillus niger Van Tieghem, were evaluated for their potential to produce lytic enzymes during in vitro antagonism. T. viride 60 inhibited highest (86.2%) growth of test fungus followed by T. harzianum 2J (80.4%) at 6 days after inoculation (DAI) on PDA media. The specific activities of chitinase, β-1,3-glucanase and protease were 11, 3.46 and 9 folds higher in T6 antagonist (T. viride 60 and A. niger interactions) followed by 8.72, 2.85 and 9 folds in T8 antagonist (T. harzianum 2J and A. niger interactions), respectively, compared to the activity produced by control petri plate T13 (A. niger alone) at 6 DAI. Activity of these lytic enzymes induced in antagonists' plates comprises the growth of Trichoderma isolates. However, cellulase and poly galacturonase were found least amount in these antagonists treatment. A significant positive correlation (p=0.01) between percentage growth inhibition of test fungus and lytic enzymes - (chitinase, β-1,3-glucanase and protease) in the culture medium of antagonist treatment established a relationship to inhibit growth of fungal pathogen by increasing the levels of these enzymes. Among the Trichoderma isolates, T. viride 60 was found best strain to be used in biological control of plant pathogen A. niger.
publishDate 2012
dc.date.none.fl_str_mv 2012-03-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000100005
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dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1517-83822012000100005
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Microbiologia
publisher.none.fl_str_mv Sociedade Brasileira de Microbiologia
dc.source.none.fl_str_mv Brazilian Journal of Microbiology v.43 n.1 2012
reponame:Brazilian Journal of Microbiology
instname:Sociedade Brasileira de Microbiologia (SBM)
instacron:SBM
instname_str Sociedade Brasileira de Microbiologia (SBM)
instacron_str SBM
institution SBM
reponame_str Brazilian Journal of Microbiology
collection Brazilian Journal of Microbiology
repository.name.fl_str_mv Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)
repository.mail.fl_str_mv bjm@sbmicrobiologia.org.br||mbmartin@usp.br
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