Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Summa phytopathologica (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-54052010000200006 |
Resumo: | Isolates of Colletotrichum gloeosporioides (ISO-1, ISO-2, ISO-3, ISO-4, ISO-5 and ISO-6), the causal agent of anthracnose disease on mango fruits, were characterized by electrophoretic patterns of total proteins and esterase in polyacrylamida gel, and also, by production of extracellular enzymes on specific solid substrate. The electrophoretic analysis showed variation in number, intensity of coloration and position of the bands in the gel at each studied system tested. In contrast to the monomorphic behavior to total proteins, high esterase polymorfism was observed indicating difference among isolates. All isolates showed the activity of extracellular enzymes such as amylase, lipase, and protease with some variation among them. The proteolitic activity seemed to be more accentuated than the two other enzymes studied. |
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Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes productionMangifera indicaproteinsisoenzymeshydrolytic activityanthracnoseIsolates of Colletotrichum gloeosporioides (ISO-1, ISO-2, ISO-3, ISO-4, ISO-5 and ISO-6), the causal agent of anthracnose disease on mango fruits, were characterized by electrophoretic patterns of total proteins and esterase in polyacrylamida gel, and also, by production of extracellular enzymes on specific solid substrate. The electrophoretic analysis showed variation in number, intensity of coloration and position of the bands in the gel at each studied system tested. In contrast to the monomorphic behavior to total proteins, high esterase polymorfism was observed indicating difference among isolates. All isolates showed the activity of extracellular enzymes such as amylase, lipase, and protease with some variation among them. The proteolitic activity seemed to be more accentuated than the two other enzymes studied.Grupo Paulista de Fitopatologia2010-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-54052010000200006Summa Phytopathologica v.36 n.2 2010reponame:Summa phytopathologica (Online)instname:Grupo Paulista de Fitopatologiainstacron:GPF10.1590/S0100-54052010000200006info:eu-repo/semantics/openAccessAssis,Tereza Cristina deMenezes,MariaAndrade,Domingos Eduardo Guimarães Tavares deCoelho,Rildo Sartori Barbosaeng2010-07-20T00:00:00Zoai:scielo:S0100-54052010000200006Revistahttp://www.scielo.br/sphttps://old.scielo.br/oai/scielo-oai.phpsumma@fca.unesp.br1980-54540100-5405opendoar:2010-07-20T00:00Summa phytopathologica (Online) - Grupo Paulista de Fitopatologiafalse |
dc.title.none.fl_str_mv |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production |
title |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production |
spellingShingle |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production Assis,Tereza Cristina de Mangifera indica proteins isoenzymes hydrolytic activity anthracnose |
title_short |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production |
title_full |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production |
title_fullStr |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production |
title_full_unstemmed |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production |
title_sort |
Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production |
author |
Assis,Tereza Cristina de |
author_facet |
Assis,Tereza Cristina de Menezes,Maria Andrade,Domingos Eduardo Guimarães Tavares de Coelho,Rildo Sartori Barbosa |
author_role |
author |
author2 |
Menezes,Maria Andrade,Domingos Eduardo Guimarães Tavares de Coelho,Rildo Sartori Barbosa |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Assis,Tereza Cristina de Menezes,Maria Andrade,Domingos Eduardo Guimarães Tavares de Coelho,Rildo Sartori Barbosa |
dc.subject.por.fl_str_mv |
Mangifera indica proteins isoenzymes hydrolytic activity anthracnose |
topic |
Mangifera indica proteins isoenzymes hydrolytic activity anthracnose |
description |
Isolates of Colletotrichum gloeosporioides (ISO-1, ISO-2, ISO-3, ISO-4, ISO-5 and ISO-6), the causal agent of anthracnose disease on mango fruits, were characterized by electrophoretic patterns of total proteins and esterase in polyacrylamida gel, and also, by production of extracellular enzymes on specific solid substrate. The electrophoretic analysis showed variation in number, intensity of coloration and position of the bands in the gel at each studied system tested. In contrast to the monomorphic behavior to total proteins, high esterase polymorfism was observed indicating difference among isolates. All isolates showed the activity of extracellular enzymes such as amylase, lipase, and protease with some variation among them. The proteolitic activity seemed to be more accentuated than the two other enzymes studied. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-06-01 |
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=S0100-54052010000200006 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-54052010000200006 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0100-54052010000200006 |
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 |
Grupo Paulista de Fitopatologia |
publisher.none.fl_str_mv |
Grupo Paulista de Fitopatologia |
dc.source.none.fl_str_mv |
Summa Phytopathologica v.36 n.2 2010 reponame:Summa phytopathologica (Online) instname:Grupo Paulista de Fitopatologia instacron:GPF |
instname_str |
Grupo Paulista de Fitopatologia |
instacron_str |
GPF |
institution |
GPF |
reponame_str |
Summa phytopathologica (Online) |
collection |
Summa phytopathologica (Online) |
repository.name.fl_str_mv |
Summa phytopathologica (Online) - Grupo Paulista de Fitopatologia |
repository.mail.fl_str_mv |
summa@fca.unesp.br |
_version_ |
1754193416748531712 |