Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis

Detalhes bibliográficos
Autor(a) principal: FRANÇA, Renata Cristina da Penha
Data de Publicação: 2007
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Biblioteca Digital de Teses e Dissertações da UFRPE
Texto Completo: http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/6450
Resumo: Tisbe biminiensis is a potential live prey for many species of aquatic animals since its nutritional value is better than those found in other feed organisms commonly used in crustacean and fish larvivultures. Live food seems to be a source of exogenous enzymes which eases food digestion of fish and crustacean early life stages. The aim of this work was to study alkaline proteases from the harpacticoida copepod Tisbe biminiensis by evaluating the effects of pH, temperature and specific inhibitors on the proteolytic activity. Proteases were also studied by SDS-PAGE and zymograms. Crude extract from T. biminiensis showed a total proteolytic activity of 0.39 mU/mg of protein and tryptic activity of 2.33 mU/mg. Optima pH and temperature were 9.0 and 55oC, respectively. The enzymes were thermostable at temperature ranging from 25 to 50oC. The enzymatic activity was strongly inhibited by the trypsin specific inhibitors TLCK (100%), SBTI (100%) and benzamidine (91%).However, EDTA, PMSF and b mercaptoethanol caused only a slight inhibition (35, 35 and 7%, respectively). The results show that alkaline proteases are present on crude extract of Tisbe biminiensis. The highest effects of trypsin inhibitors on enzyme activity suggest that this enzyme plays an important role in protein digestion. T. biminiensis is an important source of live prey to fish and crustacean larvae in nature and partially replace others live food commonly used in aquaculture because they contribute with both exogenous enzymes for the digestion processes and other nutrients required during development of aquatic animals and contribute to development of aquaculture.
id URPE_a3c676cb21cc462f50ede2f1940eba7b
oai_identifier_str oai:tede2:tede2/6450
network_acronym_str URPE
network_name_str Biblioteca Digital de Teses e Dissertações da UFRPE
repository_id_str
spelling BEZERRA, Ranilson de SouzaCARVALHO JUNIOR, Luiz Bezerra deSANTOS, Lília Pereira de SouzaCORREIA, Maria Tereza dos SantosGÁLVEZ, Alfredo OliveraOLIVEIRA FILHO, Eurico Cabral dehttp://lattes.cnpq.br/7080462940851695FRANÇA, Renata Cristina da Penha2017-02-20T11:52:01Z2007-05-08FRANÇA, Renata Cristina da Penha. Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis. 2007. 71 f. Dissertação (Programa de Pós-Graduação em Recursos Pesqueiros e Aquicultura) - Universidade Federal Rural de Pernambuco, Recife.http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/6450Tisbe biminiensis is a potential live prey for many species of aquatic animals since its nutritional value is better than those found in other feed organisms commonly used in crustacean and fish larvivultures. Live food seems to be a source of exogenous enzymes which eases food digestion of fish and crustacean early life stages. The aim of this work was to study alkaline proteases from the harpacticoida copepod Tisbe biminiensis by evaluating the effects of pH, temperature and specific inhibitors on the proteolytic activity. Proteases were also studied by SDS-PAGE and zymograms. Crude extract from T. biminiensis showed a total proteolytic activity of 0.39 mU/mg of protein and tryptic activity of 2.33 mU/mg. Optima pH and temperature were 9.0 and 55oC, respectively. The enzymes were thermostable at temperature ranging from 25 to 50oC. The enzymatic activity was strongly inhibited by the trypsin specific inhibitors TLCK (100%), SBTI (100%) and benzamidine (91%).However, EDTA, PMSF and b mercaptoethanol caused only a slight inhibition (35, 35 and 7%, respectively). The results show that alkaline proteases are present on crude extract of Tisbe biminiensis. The highest effects of trypsin inhibitors on enzyme activity suggest that this enzyme plays an important role in protein digestion. T. biminiensis is an important source of live prey to fish and crustacean larvae in nature and partially replace others live food commonly used in aquaculture because they contribute with both exogenous enzymes for the digestion processes and other nutrients required during development of aquatic animals and contribute to development of aquaculture.Os copépodos harpacticóides são microcrustáceos que servem como alimento vivo preferencial na natureza para diversas espécies de larvas de organismos aquáticos sendo nutricionalmente superiores quando comparados a outros alimentos vivos comumente utilizados nas larviculturas. O alimento vivo é uma importante fonte de enzimas exógenas que contribui para o processo digestivo dessas larvas que por não estarem com o sistema digestivo completamente formado, dependem das enzimas provenientes do alimento vivo para um melhor aproveitamento dos ingredientes da dieta,apresentando consequentemente melhores desempenhos na taxa de crescimento e sobrevivência. Este trabalho teve como objetivo caracterizar as proteases alcalinas do copépodo harpacticóide Tisbe biminiensis através de parâmetros cinéticos e físico-químicos como: pH e temperatura ótima, efeito de inibidores, estabilidade térmica, além da caracterização eletroforética por SDS-PAGE e zimograma. O extrato bruto do T. biminiensis apresentou uma atividade proteolítica total de 0,39 U/mg de proteínas sendo a atividade tríptica de 2,33 U/mg. A atividade enzimática apresentou uma temperatura ótima de 55ºC e pH ótimo de 9,0 e mostrou-se estável termicamente no intervalo de 25 a 50ºC. A atividade enzimática foi fortemente inibida por inibidores específicos de tripsina, TLCK (100±1%), SBTI (100±2%), benzamidina (91±10%), e não houve inibição significativa com os inibidores: EDTA (35±1%), PMSF (35±1%), b- mercaptoetanol (7±11%). Estes resultados demonstraram que a principal protease alcalina presente no extrato bruto do T. biminiensis foi a tripsina, exercendo importante papel na digestão protéica destes animais e este copépodo pode contribuir como fonte de enzimas exógenas para o processo digestivo nas larvas de organismos aquáticos.Submitted by (edna.saturno@ufrpe.br) on 2017-02-20T11:52:01Z No. of bitstreams: 1 Renata Cristina da Penha Franca.pdf: 1679353 bytes, checksum: 9703d2a013a1d783ae4e0d394ef6d0f9 (MD5)Made available in DSpace on 2017-02-20T11:52:01Z (GMT). No. of bitstreams: 1 Renata Cristina da Penha Franca.pdf: 1679353 bytes, checksum: 9703d2a013a1d783ae4e0d394ef6d0f9 (MD5) Previous issue date: 2007-05-08application/pdfporUniversidade Federal Rural de PernambucoPrograma de Pós-Graduação em Recursos Pesqueiros e AquiculturaUFRPEBrasilDepartamento de Pesca e AquiculturaProtease alcalinaTripsinaTisbe biminiensisCopépodo harpacticóideExogenous enzymesTrypsinCopepodCIENCIAS AGRARIAS::RECURSOS PESQUEIROS E ENGENHARIA DE PESCACaracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensisinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesis80217415640343225476006006007231936942857037408-6131750198709519811info:eu-repo/semantics/openAccessreponame:Biblioteca Digital de Teses e Dissertações da UFRPEinstname:Universidade Federal Rural de Pernambuco (UFRPE)instacron:UFRPELICENSElicense.txtlicense.txttext/plain; charset=utf-82165http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/6450/1/license.txtbd3efa91386c1718a7f26a329fdcb468MD51ORIGINALRenata Cristina da Penha Franca.pdfRenata Cristina da Penha Franca.pdfapplication/pdf1679353http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/6450/2/Renata+Cristina+da+Penha+Franca.pdf9703d2a013a1d783ae4e0d394ef6d0f9MD52tede2/64502017-02-20 08:52:01.645oai:tede2: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Biblioteca Digital de Teses e Dissertaçõeshttp://www.tede2.ufrpe.br:8080/tede/PUBhttp://www.tede2.ufrpe.br:8080/oai/requestbdtd@ufrpe.br ||bdtd@ufrpe.bropendoar:2017-02-20T11:52:01Biblioteca Digital de Teses e Dissertações da UFRPE - Universidade Federal Rural de Pernambuco (UFRPE)false
dc.title.por.fl_str_mv Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
title Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
spellingShingle Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
FRANÇA, Renata Cristina da Penha
Protease alcalina
Tripsina
Tisbe biminiensis
Copépodo harpacticóide
Exogenous enzymes
Trypsin
Copepod
CIENCIAS AGRARIAS::RECURSOS PESQUEIROS E ENGENHARIA DE PESCA
title_short Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
title_full Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
title_fullStr Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
title_full_unstemmed Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
title_sort Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis
author FRANÇA, Renata Cristina da Penha
author_facet FRANÇA, Renata Cristina da Penha
author_role author
dc.contributor.advisor1.fl_str_mv BEZERRA, Ranilson de Souza
dc.contributor.advisor-co1.fl_str_mv CARVALHO JUNIOR, Luiz Bezerra de
dc.contributor.advisor-co2.fl_str_mv SANTOS, Lília Pereira de Souza
dc.contributor.referee1.fl_str_mv CORREIA, Maria Tereza dos Santos
dc.contributor.referee2.fl_str_mv GÁLVEZ, Alfredo Olivera
dc.contributor.referee3.fl_str_mv OLIVEIRA FILHO, Eurico Cabral de
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/7080462940851695
dc.contributor.author.fl_str_mv FRANÇA, Renata Cristina da Penha
contributor_str_mv BEZERRA, Ranilson de Souza
CARVALHO JUNIOR, Luiz Bezerra de
SANTOS, Lília Pereira de Souza
CORREIA, Maria Tereza dos Santos
GÁLVEZ, Alfredo Olivera
OLIVEIRA FILHO, Eurico Cabral de
dc.subject.por.fl_str_mv Protease alcalina
Tripsina
Tisbe biminiensis
Copépodo harpacticóide
topic Protease alcalina
Tripsina
Tisbe biminiensis
Copépodo harpacticóide
Exogenous enzymes
Trypsin
Copepod
CIENCIAS AGRARIAS::RECURSOS PESQUEIROS E ENGENHARIA DE PESCA
dc.subject.eng.fl_str_mv Exogenous enzymes
Trypsin
Copepod
dc.subject.cnpq.fl_str_mv CIENCIAS AGRARIAS::RECURSOS PESQUEIROS E ENGENHARIA DE PESCA
description Tisbe biminiensis is a potential live prey for many species of aquatic animals since its nutritional value is better than those found in other feed organisms commonly used in crustacean and fish larvivultures. Live food seems to be a source of exogenous enzymes which eases food digestion of fish and crustacean early life stages. The aim of this work was to study alkaline proteases from the harpacticoida copepod Tisbe biminiensis by evaluating the effects of pH, temperature and specific inhibitors on the proteolytic activity. Proteases were also studied by SDS-PAGE and zymograms. Crude extract from T. biminiensis showed a total proteolytic activity of 0.39 mU/mg of protein and tryptic activity of 2.33 mU/mg. Optima pH and temperature were 9.0 and 55oC, respectively. The enzymes were thermostable at temperature ranging from 25 to 50oC. The enzymatic activity was strongly inhibited by the trypsin specific inhibitors TLCK (100%), SBTI (100%) and benzamidine (91%).However, EDTA, PMSF and b mercaptoethanol caused only a slight inhibition (35, 35 and 7%, respectively). The results show that alkaline proteases are present on crude extract of Tisbe biminiensis. The highest effects of trypsin inhibitors on enzyme activity suggest that this enzyme plays an important role in protein digestion. T. biminiensis is an important source of live prey to fish and crustacean larvae in nature and partially replace others live food commonly used in aquaculture because they contribute with both exogenous enzymes for the digestion processes and other nutrients required during development of aquatic animals and contribute to development of aquaculture.
publishDate 2007
dc.date.issued.fl_str_mv 2007-05-08
dc.date.accessioned.fl_str_mv 2017-02-20T11:52:01Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.citation.fl_str_mv FRANÇA, Renata Cristina da Penha. Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis. 2007. 71 f. Dissertação (Programa de Pós-Graduação em Recursos Pesqueiros e Aquicultura) - Universidade Federal Rural de Pernambuco, Recife.
dc.identifier.uri.fl_str_mv http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/6450
identifier_str_mv FRANÇA, Renata Cristina da Penha. Caracterização da atividade tríptica do copépodo harpacticoida Tisbe biminiensis. 2007. 71 f. Dissertação (Programa de Pós-Graduação em Recursos Pesqueiros e Aquicultura) - Universidade Federal Rural de Pernambuco, Recife.
url http://www.tede2.ufrpe.br:8080/tede2/handle/tede2/6450
dc.language.iso.fl_str_mv por
language por
dc.relation.program.fl_str_mv 8021741564034322547
dc.relation.confidence.fl_str_mv 600
600
600
dc.relation.department.fl_str_mv 7231936942857037408
dc.relation.cnpq.fl_str_mv -6131750198709519811
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 Universidade Federal Rural de Pernambuco
dc.publisher.program.fl_str_mv Programa de Pós-Graduação em Recursos Pesqueiros e Aquicultura
dc.publisher.initials.fl_str_mv UFRPE
dc.publisher.country.fl_str_mv Brasil
dc.publisher.department.fl_str_mv Departamento de Pesca e Aquicultura
publisher.none.fl_str_mv Universidade Federal Rural de Pernambuco
dc.source.none.fl_str_mv reponame:Biblioteca Digital de Teses e Dissertações da UFRPE
instname:Universidade Federal Rural de Pernambuco (UFRPE)
instacron:UFRPE
instname_str Universidade Federal Rural de Pernambuco (UFRPE)
instacron_str UFRPE
institution UFRPE
reponame_str Biblioteca Digital de Teses e Dissertações da UFRPE
collection Biblioteca Digital de Teses e Dissertações da UFRPE
bitstream.url.fl_str_mv http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/6450/1/license.txt
http://www.tede2.ufrpe.br:8080/tede2/bitstream/tede2/6450/2/Renata+Cristina+da+Penha+Franca.pdf
bitstream.checksum.fl_str_mv bd3efa91386c1718a7f26a329fdcb468
9703d2a013a1d783ae4e0d394ef6d0f9
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
repository.name.fl_str_mv Biblioteca Digital de Teses e Dissertações da UFRPE - Universidade Federal Rural de Pernambuco (UFRPE)
repository.mail.fl_str_mv bdtd@ufrpe.br ||bdtd@ufrpe.br
_version_ 1791083583434129408