Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger
Autor(a) principal: | |
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Data de Publicação: | 2007 |
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/1822/7472 |
Resumo: | Ochratoxin A is a mycotoxin produced by several Aspergillus and some Penicillium species which may be present in food and feed products. It can be enzymatically hydrolyzed into ochratoxin α and l-β-phenylalanine, thereby decreasing its toxicity. The ochratoxin A degradation capacity of Aspergillus niger is well known and here we report the isolation and purification of a novel enzyme from A. niger that hydrolyzes this mycotoxin. A wheat germ medium supplemented with ochratoxin A was used to produce the enzyme, which was purified from culture filtrate by acetone precipitation and anion exchange chromatography. An overall purification of 2.5-fold with a recovery of 68% and a final specific activity of 36 U/mg was obtained. The enzyme is a metalloenzyme as it was inhibited at 10 mM EDTA, whereas PMSF had no effect. The ochratoxin A hydrolytic enzyme presented a V max of 0.44 μM/min and a K m of 0.5 mM when the reaction was carried out at pH 7.5 and 37°C. |
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Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus nigerAspergillus nigerCarboxypeptidaseDegradationOchratoxin AOchratoxin αScience & TechnologyOchratoxin A is a mycotoxin produced by several Aspergillus and some Penicillium species which may be present in food and feed products. It can be enzymatically hydrolyzed into ochratoxin α and l-β-phenylalanine, thereby decreasing its toxicity. The ochratoxin A degradation capacity of Aspergillus niger is well known and here we report the isolation and purification of a novel enzyme from A. niger that hydrolyzes this mycotoxin. A wheat germ medium supplemented with ochratoxin A was used to produce the enzyme, which was purified from culture filtrate by acetone precipitation and anion exchange chromatography. An overall purification of 2.5-fold with a recovery of 68% and a final specific activity of 36 U/mg was obtained. The enzyme is a metalloenzyme as it was inhibited at 10 mM EDTA, whereas PMSF had no effect. The ochratoxin A hydrolytic enzyme presented a V max of 0.44 μM/min and a K m of 0.5 mM when the reaction was carried out at pH 7.5 and 37°C.Fundação para a Ciência e a Tecnologia (FCT)SpringerUniversidade do MinhoAbrunhosa, LuísVenâncio, Armando2007-122007-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/7472eng"Biotechnology Letters." ISSN 0141-5492. 29:12 (Dez. 2007) p. 1909-1914.0141-549210.1007/s10529-007-9479-217653510info: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:RCAAP2024-05-11T04:34:38Zoai:repositorium.sdum.uminho.pt:1822/7472Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-11T04:34:38Repositório 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 |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger |
title |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger |
spellingShingle |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger Abrunhosa, Luís Aspergillus niger Carboxypeptidase Degradation Ochratoxin A Ochratoxin α Science & Technology |
title_short |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger |
title_full |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger |
title_fullStr |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger |
title_full_unstemmed |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger |
title_sort |
Isolation and purification of an enzyme hydrolyzing ochratoxin A from aspergillus niger |
author |
Abrunhosa, Luís |
author_facet |
Abrunhosa, Luís Venâncio, Armando |
author_role |
author |
author2 |
Venâncio, Armando |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Abrunhosa, Luís Venâncio, Armando |
dc.subject.por.fl_str_mv |
Aspergillus niger Carboxypeptidase Degradation Ochratoxin A Ochratoxin α Science & Technology |
topic |
Aspergillus niger Carboxypeptidase Degradation Ochratoxin A Ochratoxin α Science & Technology |
description |
Ochratoxin A is a mycotoxin produced by several Aspergillus and some Penicillium species which may be present in food and feed products. It can be enzymatically hydrolyzed into ochratoxin α and l-β-phenylalanine, thereby decreasing its toxicity. The ochratoxin A degradation capacity of Aspergillus niger is well known and here we report the isolation and purification of a novel enzyme from A. niger that hydrolyzes this mycotoxin. A wheat germ medium supplemented with ochratoxin A was used to produce the enzyme, which was purified from culture filtrate by acetone precipitation and anion exchange chromatography. An overall purification of 2.5-fold with a recovery of 68% and a final specific activity of 36 U/mg was obtained. The enzyme is a metalloenzyme as it was inhibited at 10 mM EDTA, whereas PMSF had no effect. The ochratoxin A hydrolytic enzyme presented a V max of 0.44 μM/min and a K m of 0.5 mM when the reaction was carried out at pH 7.5 and 37°C. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-12 2007-12-01T00:00:00Z |
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/1822/7472 |
url |
http://hdl.handle.net/1822/7472 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Biotechnology Letters." ISSN 0141-5492. 29:12 (Dez. 2007) p. 1909-1914. 0141-5492 10.1007/s10529-007-9479-2 17653510 |
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 |
instname_str |
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 |
mluisa.alvim@gmail.com |
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1817544353853210624 |