Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens

Detalhes bibliográficos
Autor(a) principal: Silva, Germana Michelle de Medeiros e
Data de Publicação: 2016
Outros Autores: Bezerra, Raquel Pedrosa, Teixeira, J. A., Silva, Flávio Oliveira, Correia, Juliana Mendes, Porto, Tatiana Souza, Lima-Filho, José Luis, Porto, Ana Lúcia Figueiredo
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/47493
Resumo: Thrombosis is a pathophysiological disorder caused by accumulation of fibrin in the blood. Fibrinolytic proteases with potent thrombolytic activity have been produced by diverse microbial sources. Considering the microbial biodiversity of the Amazon region, this study aimed at the screening, production and biochemical characterization of a fibrinolytic enzyme produced by Streptomyces sp. isolated from Amazonian lichens. The strain Streptomyces DPUA1576 showed the highest fibrinolytic activity, which was 283 mm2. Three variables at two levels were used to assess their effects on the fibrinolytic production. The parameters studied were agitation (0.28 - 1.12 g), temperature (28 - 36 ºC) and pH (6.0 - 8.0); all of them had significant effects on the fibrinolytic production. The maximum fibrinolytic activity (304 mm2) was observed at 1.12 g, 28 ºC, and pH of 8.0. The crude extract of the fermentation broth was used to assess the biochemical properties of the enzyme. Protease and fibrinolytic activities were stable during 6 h, at a pH ranging from 6.8 to 8.4 and 5.8 to 9.2, respectively. Optimum temperature for protease activity ranged between 35 and 55 °C, while the highest fibrinolytic activity was observed at 45 ºC. Proteolytic activity was inhibited by Cu2+ and Co2+ ions, phenylmethylsulfonyl fluoride (PMSF) and pepstatin A, which suggests that the enzyme is a serine protease. Enzymatic extract cleaved fibrinogen at the subunits A-chain, A-chain, and -chain. The results indicated that Streptomyces sp. DPUA 1576 produces enzymes with fibrinolytic and fibrinogenolytic activity, enzymes with an important application in the pharmaceutical industry.
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spelling Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichensActinomycetesfibrinolytic proteaseinhibitor proteasefibrinogenolytic activityScience & TechnologyThrombosis is a pathophysiological disorder caused by accumulation of fibrin in the blood. Fibrinolytic proteases with potent thrombolytic activity have been produced by diverse microbial sources. Considering the microbial biodiversity of the Amazon region, this study aimed at the screening, production and biochemical characterization of a fibrinolytic enzyme produced by Streptomyces sp. isolated from Amazonian lichens. The strain Streptomyces DPUA1576 showed the highest fibrinolytic activity, which was 283 mm2. Three variables at two levels were used to assess their effects on the fibrinolytic production. The parameters studied were agitation (0.28 - 1.12 g), temperature (28 - 36 ºC) and pH (6.0 - 8.0); all of them had significant effects on the fibrinolytic production. The maximum fibrinolytic activity (304 mm2) was observed at 1.12 g, 28 ºC, and pH of 8.0. The crude extract of the fermentation broth was used to assess the biochemical properties of the enzyme. Protease and fibrinolytic activities were stable during 6 h, at a pH ranging from 6.8 to 8.4 and 5.8 to 9.2, respectively. Optimum temperature for protease activity ranged between 35 and 55 °C, while the highest fibrinolytic activity was observed at 45 ºC. Proteolytic activity was inhibited by Cu2+ and Co2+ ions, phenylmethylsulfonyl fluoride (PMSF) and pepstatin A, which suggests that the enzyme is a serine protease. Enzymatic extract cleaved fibrinogen at the subunits A-chain, A-chain, and -chain. The results indicated that Streptomyces sp. DPUA 1576 produces enzymes with fibrinolytic and fibrinogenolytic activity, enzymes with an important application in the pharmaceutical industry.The authors grateful acknowledge the financial support of Fundação de Amparo a Pesquisa do Estado de Pernambuco (FACEPE, Pernambuco, Brazil, N. 0158-2.12/11), CNPq/ RENORBIO (National Counsel of Technological and Scientific Development, N.55146/2010-3) and National Council for the Improvement of Higher Education (CAPES, Brazil) for the scholarship. The author thanks editor and reviewers for their review and comments.info:eu-repo/semantics/publishedVersionInstituto Nacional de Pesquisas da AmazôniaUniversidade do MinhoSilva, Germana Michelle de Medeiros eBezerra, Raquel PedrosaTeixeira, J. A.Silva, Flávio OliveiraCorreia, Juliana MendesPorto, Tatiana SouzaLima-Filho, José LuisPorto, Ana Lúcia Figueiredo2016-092016-09-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/47493engSilva, Germana Michelle de Medeiros e; Bezerra, Raquel Pedrosa; Teixeira, José A.; Silva, Flávio Oliveira; Correia, Juliana Mendes; Porto, Tatiana Souza; Lima-Filho, José Luis; Porto, Ana Lúcia Figueiredo, Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens. Acta Amazonica, 46, 323-332, 20160044-59671809-439210.1590/1809-4392201600022http://www.scielo.br/scielo.php?script=sci_serial&pid=0044-5967&lng=en&nrm=isoinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:09:44Zoai:repositorium.sdum.uminho.pt:1822/47493Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:01:14.527798Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
title Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
spellingShingle Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
Silva, Germana Michelle de Medeiros e
Actinomycetes
fibrinolytic protease
inhibitor protease
fibrinogenolytic activity
Science & Technology
title_short Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
title_full Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
title_fullStr Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
title_full_unstemmed Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
title_sort Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
author Silva, Germana Michelle de Medeiros e
author_facet Silva, Germana Michelle de Medeiros e
Bezerra, Raquel Pedrosa
Teixeira, J. A.
Silva, Flávio Oliveira
Correia, Juliana Mendes
Porto, Tatiana Souza
Lima-Filho, José Luis
Porto, Ana Lúcia Figueiredo
author_role author
author2 Bezerra, Raquel Pedrosa
Teixeira, J. A.
Silva, Flávio Oliveira
Correia, Juliana Mendes
Porto, Tatiana Souza
Lima-Filho, José Luis
Porto, Ana Lúcia Figueiredo
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Silva, Germana Michelle de Medeiros e
Bezerra, Raquel Pedrosa
Teixeira, J. A.
Silva, Flávio Oliveira
Correia, Juliana Mendes
Porto, Tatiana Souza
Lima-Filho, José Luis
Porto, Ana Lúcia Figueiredo
dc.subject.por.fl_str_mv Actinomycetes
fibrinolytic protease
inhibitor protease
fibrinogenolytic activity
Science & Technology
topic Actinomycetes
fibrinolytic protease
inhibitor protease
fibrinogenolytic activity
Science & Technology
description Thrombosis is a pathophysiological disorder caused by accumulation of fibrin in the blood. Fibrinolytic proteases with potent thrombolytic activity have been produced by diverse microbial sources. Considering the microbial biodiversity of the Amazon region, this study aimed at the screening, production and biochemical characterization of a fibrinolytic enzyme produced by Streptomyces sp. isolated from Amazonian lichens. The strain Streptomyces DPUA1576 showed the highest fibrinolytic activity, which was 283 mm2. Three variables at two levels were used to assess their effects on the fibrinolytic production. The parameters studied were agitation (0.28 - 1.12 g), temperature (28 - 36 ºC) and pH (6.0 - 8.0); all of them had significant effects on the fibrinolytic production. The maximum fibrinolytic activity (304 mm2) was observed at 1.12 g, 28 ºC, and pH of 8.0. The crude extract of the fermentation broth was used to assess the biochemical properties of the enzyme. Protease and fibrinolytic activities were stable during 6 h, at a pH ranging from 6.8 to 8.4 and 5.8 to 9.2, respectively. Optimum temperature for protease activity ranged between 35 and 55 °C, while the highest fibrinolytic activity was observed at 45 ºC. Proteolytic activity was inhibited by Cu2+ and Co2+ ions, phenylmethylsulfonyl fluoride (PMSF) and pepstatin A, which suggests that the enzyme is a serine protease. Enzymatic extract cleaved fibrinogen at the subunits A-chain, A-chain, and -chain. The results indicated that Streptomyces sp. DPUA 1576 produces enzymes with fibrinolytic and fibrinogenolytic activity, enzymes with an important application in the pharmaceutical industry.
publishDate 2016
dc.date.none.fl_str_mv 2016-09
2016-09-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/47493
url http://hdl.handle.net/1822/47493
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Silva, Germana Michelle de Medeiros e; Bezerra, Raquel Pedrosa; Teixeira, José A.; Silva, Flávio Oliveira; Correia, Juliana Mendes; Porto, Tatiana Souza; Lima-Filho, José Luis; Porto, Ana Lúcia Figueiredo, Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens. Acta Amazonica, 46, 323-332, 2016
0044-5967
1809-4392
10.1590/1809-4392201600022
http://www.scielo.br/scielo.php?script=sci_serial&pid=0044-5967&lng=en&nrm=iso
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Instituto Nacional de Pesquisas da Amazônia
publisher.none.fl_str_mv Instituto Nacional de Pesquisas da Amazônia
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
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instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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