Transglutaminases: recent achievements and new sources
Autor(a) principal: | |
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Data de Publicação: | 2014 |
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/10198/10578 |
Resumo: | Transglutaminases are a family of enzymes (EC 2.3.2.13), widely distributed in various organs, tissues, and body fluids, that catalyze the formation of a covalent bond between a free amine group and the γ-carboxamide group of protein or peptide-bound glutamine. Besides forming these bonds, that exhibit high resistance to proteolytic degradation, transglutaminases also form extensively cross-linked, generally insoluble, protein biopolymers that are indispensable for the organism to create barriers and stable structures. The extremely high cost of transglutaminase of animal origin has hampered its wider application and has initiated efforts to find an enzyme of microbial origin. Since the early 1990s, many microbial transglutaminase-producing strains have been found, and production processes have been optimized. This has resulted in a rapidly increasing number of applications of transglutaminase in the food sector. However, applications of microbial transglutaminase in other sectors have also been explored, but in a much lesser extent. Our group has identified a transglutaminase in the oomycete Phytophthora cinnamomi, which is able to induct defense responses and disease-like symptoms. In this mini-review, we report the achievements in this area in order to illustrate the importance and the versatility of transglutaminases. |
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Transglutaminases: recent achievements and new sourcesTransglutaminaseMTGPhytophthora cinnamomiApplicationsTransglutaminases are a family of enzymes (EC 2.3.2.13), widely distributed in various organs, tissues, and body fluids, that catalyze the formation of a covalent bond between a free amine group and the γ-carboxamide group of protein or peptide-bound glutamine. Besides forming these bonds, that exhibit high resistance to proteolytic degradation, transglutaminases also form extensively cross-linked, generally insoluble, protein biopolymers that are indispensable for the organism to create barriers and stable structures. The extremely high cost of transglutaminase of animal origin has hampered its wider application and has initiated efforts to find an enzyme of microbial origin. Since the early 1990s, many microbial transglutaminase-producing strains have been found, and production processes have been optimized. This has resulted in a rapidly increasing number of applications of transglutaminase in the food sector. However, applications of microbial transglutaminase in other sectors have also been explored, but in a much lesser extent. Our group has identified a transglutaminase in the oomycete Phytophthora cinnamomi, which is able to induct defense responses and disease-like symptoms. In this mini-review, we report the achievements in this area in order to illustrate the importance and the versatility of transglutaminases.SpringerBiblioteca Digital do IPBMartins, IvoneMatos, MauroCosta, Rodrigo Arthur FonsecaSilva, Fátima H.Pascoal, AnaniasEstevinho, Leticia M.Choupina, Altino2014-09-24T14:34:03Z20142014-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10198/10578engMartins, Ivone; Matos, Mauro; Costa, Rodrigo; Silva, Fátima; Pascoal, Ananias; Estevinho, Leticia M.; Choupina, Altino (2014). Transglutaminases: recent achievements and new sources. Applied Microbiology and Biotechnology. ISSN 0175-7598. 98:16, p. 6957-69640175-759810.1007/s00253-014-5894-1info: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:RCAAP2023-11-21T10:25:03Zoai:bibliotecadigital.ipb.pt:10198/10578Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:01:22.383328Repositório 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 |
Transglutaminases: recent achievements and new sources |
title |
Transglutaminases: recent achievements and new sources |
spellingShingle |
Transglutaminases: recent achievements and new sources Martins, Ivone Transglutaminase MTG Phytophthora cinnamomi Applications |
title_short |
Transglutaminases: recent achievements and new sources |
title_full |
Transglutaminases: recent achievements and new sources |
title_fullStr |
Transglutaminases: recent achievements and new sources |
title_full_unstemmed |
Transglutaminases: recent achievements and new sources |
title_sort |
Transglutaminases: recent achievements and new sources |
author |
Martins, Ivone |
author_facet |
Martins, Ivone Matos, Mauro Costa, Rodrigo Arthur Fonseca Silva, Fátima H. Pascoal, Ananias Estevinho, Leticia M. Choupina, Altino |
author_role |
author |
author2 |
Matos, Mauro Costa, Rodrigo Arthur Fonseca Silva, Fátima H. Pascoal, Ananias Estevinho, Leticia M. Choupina, Altino |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Biblioteca Digital do IPB |
dc.contributor.author.fl_str_mv |
Martins, Ivone Matos, Mauro Costa, Rodrigo Arthur Fonseca Silva, Fátima H. Pascoal, Ananias Estevinho, Leticia M. Choupina, Altino |
dc.subject.por.fl_str_mv |
Transglutaminase MTG Phytophthora cinnamomi Applications |
topic |
Transglutaminase MTG Phytophthora cinnamomi Applications |
description |
Transglutaminases are a family of enzymes (EC 2.3.2.13), widely distributed in various organs, tissues, and body fluids, that catalyze the formation of a covalent bond between a free amine group and the γ-carboxamide group of protein or peptide-bound glutamine. Besides forming these bonds, that exhibit high resistance to proteolytic degradation, transglutaminases also form extensively cross-linked, generally insoluble, protein biopolymers that are indispensable for the organism to create barriers and stable structures. The extremely high cost of transglutaminase of animal origin has hampered its wider application and has initiated efforts to find an enzyme of microbial origin. Since the early 1990s, many microbial transglutaminase-producing strains have been found, and production processes have been optimized. This has resulted in a rapidly increasing number of applications of transglutaminase in the food sector. However, applications of microbial transglutaminase in other sectors have also been explored, but in a much lesser extent. Our group has identified a transglutaminase in the oomycete Phytophthora cinnamomi, which is able to induct defense responses and disease-like symptoms. In this mini-review, we report the achievements in this area in order to illustrate the importance and the versatility of transglutaminases. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-09-24T14:34:03Z 2014 2014-01-01T00:00:00Z |
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/10198/10578 |
url |
http://hdl.handle.net/10198/10578 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Martins, Ivone; Matos, Mauro; Costa, Rodrigo; Silva, Fátima; Pascoal, Ananias; Estevinho, Leticia M.; Choupina, Altino (2014). Transglutaminases: recent achievements and new sources. Applied Microbiology and Biotechnology. ISSN 0175-7598. 98:16, p. 6957-6964 0175-7598 10.1007/s00253-014-5894-1 |
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 |
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RCAAP |
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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 |
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1817551576444698624 |