Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/25532 |
Resumo: | Fibrinolytic proteases are enzymes that degrade fibrin; these enzymes are a promising alternative for thrombolytic therapy, and microorganisms produce them. The aim of this study was to evaluate the optimum conditions for the integrated production and purification of fibrinolytic protease from Bacillus sp. UFPEDA 485. Extractive fermentation was carried out in a culture medium containing soybean flour and by adding polyethylene glycol (PEG) and Na2SO4 according to a 23 experimental design. In all assays, the enzyme preferentially partitioned to the bottom phase (K < 1), with an optimum activity of 835 U ml−1 in the bottom phase (salt-rich phase). The best conditions for extractive fermentation were obtained with 18 % PEG 8000 and 13 % Na2SO4. Characterization showed that it is a metalloprotease, as a strong inhibition—residual activity of 3.13 %—occurred in the presence of ethylenediaminetetraacetic acid. It was also observed that enzymatic activity was stimulated in the presence of ions: CaCl2 (440 %), MgCl2 (440 %), FeSO4 (268 %), and KCl (268 %). The obtained results indicate that the use of a low-cost substrate and the integration of fermentation with an aqueous two-phase system extraction may be an interesting alternative for the production of fibrinolytic protease. |
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Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485Fibrinolytic proteaseBacillusPEG/sodium sulfateATPSExtractive fermentationScience & TechnologyFibrinolytic proteases are enzymes that degrade fibrin; these enzymes are a promising alternative for thrombolytic therapy, and microorganisms produce them. The aim of this study was to evaluate the optimum conditions for the integrated production and purification of fibrinolytic protease from Bacillus sp. UFPEDA 485. Extractive fermentation was carried out in a culture medium containing soybean flour and by adding polyethylene glycol (PEG) and Na2SO4 according to a 23 experimental design. In all assays, the enzyme preferentially partitioned to the bottom phase (K < 1), with an optimum activity of 835 U ml−1 in the bottom phase (salt-rich phase). The best conditions for extractive fermentation were obtained with 18 % PEG 8000 and 13 % Na2SO4. Characterization showed that it is a metalloprotease, as a strong inhibition—residual activity of 3.13 %—occurred in the presence of ethylenediaminetetraacetic acid. It was also observed that enzymatic activity was stimulated in the presence of ions: CaCl2 (440 %), MgCl2 (440 %), FeSO4 (268 %), and KCl (268 %). The obtained results indicate that the use of a low-cost substrate and the integration of fermentation with an aqueous two-phase system extraction may be an interesting alternative for the production of fibrinolytic protease.The authors thank CAPES (National Council for the Improvement of Higher Education) for the scholarship and CNPq (National Counsel of Technological and Scientific Development) and RENORBIO for the financial support.SpringerUniversidade do MinhoSales, Amanda EmmanuelleSouza, Fabiana América Silva Dantas deTeixeira, J. A.Porto, Tatiana SouzaPorto, Ana L. F.20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/25532eng0273-22890273-228910.1007/s12010-013-0306-z23716141info: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:RCAAP2023-07-21T12:41:20Zoai:repositorium.sdum.uminho.pt:1822/25532Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:38:18.244456Repositório 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 |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 |
title |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 |
spellingShingle |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 Sales, Amanda Emmanuelle Fibrinolytic protease Bacillus PEG/sodium sulfate ATPS Extractive fermentation Science & Technology |
title_short |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 |
title_full |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 |
title_fullStr |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 |
title_full_unstemmed |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 |
title_sort |
Integrated process production and extraction of the fibrinolytic protease from Bacillus sp. UFPEDA 485 |
author |
Sales, Amanda Emmanuelle |
author_facet |
Sales, Amanda Emmanuelle Souza, Fabiana América Silva Dantas de Teixeira, J. A. Porto, Tatiana Souza Porto, Ana L. F. |
author_role |
author |
author2 |
Souza, Fabiana América Silva Dantas de Teixeira, J. A. Porto, Tatiana Souza Porto, Ana L. F. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Sales, Amanda Emmanuelle Souza, Fabiana América Silva Dantas de Teixeira, J. A. Porto, Tatiana Souza Porto, Ana L. F. |
dc.subject.por.fl_str_mv |
Fibrinolytic protease Bacillus PEG/sodium sulfate ATPS Extractive fermentation Science & Technology |
topic |
Fibrinolytic protease Bacillus PEG/sodium sulfate ATPS Extractive fermentation Science & Technology |
description |
Fibrinolytic proteases are enzymes that degrade fibrin; these enzymes are a promising alternative for thrombolytic therapy, and microorganisms produce them. The aim of this study was to evaluate the optimum conditions for the integrated production and purification of fibrinolytic protease from Bacillus sp. UFPEDA 485. Extractive fermentation was carried out in a culture medium containing soybean flour and by adding polyethylene glycol (PEG) and Na2SO4 according to a 23 experimental design. In all assays, the enzyme preferentially partitioned to the bottom phase (K < 1), with an optimum activity of 835 U ml−1 in the bottom phase (salt-rich phase). The best conditions for extractive fermentation were obtained with 18 % PEG 8000 and 13 % Na2SO4. Characterization showed that it is a metalloprotease, as a strong inhibition—residual activity of 3.13 %—occurred in the presence of ethylenediaminetetraacetic acid. It was also observed that enzymatic activity was stimulated in the presence of ions: CaCl2 (440 %), MgCl2 (440 %), FeSO4 (268 %), and KCl (268 %). The obtained results indicate that the use of a low-cost substrate and the integration of fermentation with an aqueous two-phase system extraction may be an interesting alternative for the production of fibrinolytic protease. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 2013-01-01T00:00:00Z |
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/1822/25532 |
url |
http://hdl.handle.net/1822/25532 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0273-2289 0273-2289 10.1007/s12010-013-0306-z 23716141 |
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 |
Springer |
publisher.none.fl_str_mv |
Springer |
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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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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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1799132919493558272 |