Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)

Detalhes bibliográficos
Ano de defesa: 2019
Autor(a) principal: Cruz, Wellington Oliveira da lattes
Orientador(a): Pontes, Emerson Guedes
Banca de defesa: Pontes, Emerson Guedes, Souza, Cristiane Martins de, Santos, Danielle M. P. de Oliveira, Mesquita, Rafael Dias, Sant`Anna, Carlos Mauricio
Tipo de documento: Tese
Tipo de acesso: Acesso aberto
Idioma: por
Instituição de defesa: Universidade Federal Rural do Rio de Janeiro
Programa de Pós-Graduação: Programa de P?s-Gradua??o em Qu?mica
Departamento: Instituto de Qu?mica
País: Brasil
Palavras-chave em Português:
Inseto
Dietas
Proteases
Alphitobius diaperinus
Palavras-chave em Inglês:
Insect
Diets
Proteases
Área do conhecimento CNPq:
Qu?mica
Link de acesso: https://tede.ufrrj.br/jspui/handle/jspui/5822
Resumo: Alphitobius diaperinus is considered an important issue in the avian environment. Studying your behavior, eating habits and digestive enzymes may indicate important targets in your control. Control of A. diaperinus is considered difficult, its natural enemies are little known, and the use of chemical insecticides is the main method of control. Insect digestive proteases catalyze the production of peptides and amino acids from a protein diet and they are found in the midgut region of insects. Proteolytic activities in the digestive tract of A. diper?nus larvae and adults were determined using azocasein and specific substrates after feeding on different diets. The crude extract of the digestive tract of A. diaperinus larvae showed activity on azocasein and Abz-Phe-Arg-MCA. It was inhibited by more than 50% by E-64 and activated by 2.0 mM DTT at acid pH. Nine bands were detected with proteolytic activity and molecular mass in the range 10 kDa - 100 kDa through zymogram, using 0.1% gelatin as substrate. Different classes of proteases were identified in the presence of classical protease inhibitors such as E-64, iodoacetamide and iodoacetic acid, PMSF, SBTI, aprotinin and TLCK. A higher level of proteolytic activity was observed at pHs between 5 and 6. Although combinations of serine and cysteine proteases have been observed, acid proteases showed higher levels of proteolytic activity. Calcium ion increased the protease activity at concentrations greater than 2.0 mM. Two-dimensional nano-HPLC and ESI-MS / MS analyzes resulted in the identification of proteases such as tripine, cathepsins, metalloproteases, aminopeptidases, peptidases and dipeptidases. High inhibitory potential of different series of imidazolone on cysteine protease was observed, what can be used as control tools of A. diaperinus.
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spelling Pontes, Emerson Guedes045.534.107-96Pontes, Emerson GuedesSouza, Cristiane Martins deSantos, Danielle M. P. de OliveiraMesquita, Rafael DiasSant`Anna, Carlos Mauricio075.736.047-50http://lattes.cnpq.br/5335761763028967Cruz, Wellington Oliveira da2022-07-27T16:56:47Z2019-08-06CRUZ, Wellington Oliveira. Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae). 2019. 168 f. Tese (Doutorado em Qu?mica) - Instituto de Qu?mica, Universidade Federal Rural do Rio de Janeiro, Serop?dica, 2019.https://tede.ufrrj.br/jspui/handle/jspui/5822Alphitobius diaperinus is considered an important issue in the avian environment. Studying your behavior, eating habits and digestive enzymes may indicate important targets in your control. Control of A. diaperinus is considered difficult, its natural enemies are little known, and the use of chemical insecticides is the main method of control. Insect digestive proteases catalyze the production of peptides and amino acids from a protein diet and they are found in the midgut region of insects. Proteolytic activities in the digestive tract of A. diper?nus larvae and adults were determined using azocasein and specific substrates after feeding on different diets. The crude extract of the digestive tract of A. diaperinus larvae showed activity on azocasein and Abz-Phe-Arg-MCA. It was inhibited by more than 50% by E-64 and activated by 2.0 mM DTT at acid pH. Nine bands were detected with proteolytic activity and molecular mass in the range 10 kDa - 100 kDa through zymogram, using 0.1% gelatin as substrate. Different classes of proteases were identified in the presence of classical protease inhibitors such as E-64, iodoacetamide and iodoacetic acid, PMSF, SBTI, aprotinin and TLCK. A higher level of proteolytic activity was observed at pHs between 5 and 6. Although combinations of serine and cysteine proteases have been observed, acid proteases showed higher levels of proteolytic activity. Calcium ion increased the protease activity at concentrations greater than 2.0 mM. Two-dimensional nano-HPLC and ESI-MS / MS analyzes resulted in the identification of proteases such as tripine, cathepsins, metalloproteases, aminopeptidases, peptidases and dipeptidases. High inhibitory potential of different series of imidazolone on cysteine protease was observed, what can be used as control tools of A. diaperinus.O Alphitobius diaperinus ? considerado uma praga importante em ambiente avi?rio. O estudo do seu comportamento, h?bitos alimentares e enzimas digestivas, podem indicar alvos importantes no seu controle. O controle do A. diaperinus ? considerado dif?cil, seus inimigos naturais s?o pouco conhecidos e sendo o uso de inseticidas qu?mico o principal m?todo de controle. Proteases digestivas de insetos catalisam a produ??o de pept?deos e amino?cidos a partir de uma dieta prot?ica e s?o encontradas na regi?o do intestino m?dio dos insetos. As atividades proteol?ticas no trato digestivo das larvas e adultos de A. diperinus foram determinadas utilizando azocase?na e substratos especificos ap?s alimentarem-se de diferentes dietas. O extrato bruto do homogeneizado do trato digestivo das larvas A. diaperinus mostrou atividade sobre azocase?na e Abz-Phe-Arg-MCA e foi inibida em mais de 50% pelo inibidor da ciste?no protease E-64 e foi ativado por DTT 2,0 mM em pH ?cido. Nove bandas foram detectadas com atividade proteol?tica e massa molecular na faixa 10 kDa ? 100 kDa atrav?s de zimograma, utilizando gelatina 0,1% como substrato. Diferentes classes de proteases foram identificadas na presen?a de inibidores de proteases cl?ssicos como E-64, iodoacetamida e ?cido iodoac?tico, PMSF, SBTI, aprotinina e TLCK. Foi observado maior n?vel de atividade proteol?tica em pHs entre 5 e 6. Embora tenham sido observadas combina??es de proteases de serina e ciste?na, as proteases ?cidas apresentaram n?veis mais altos de atividade proteol?tica. O c?lcio aumentou a atividade proteasica em concentra??es maiores que 2,0 mM. An?lises de nano-HPLC bidimensional e ESI-MS/MS resultaram na identifica??o de proteases como tripsina, catepsinas, metaloproteases, aminopeptidases, peptidases e dipeptidases. Foi observado alto potencial inibit?rio de diferentes s?ries de imidazolonas sobre atividade ciste?no proteases, a qual pode ser utilizada como ferramentas de controle do A. diaperinus.Submitted by Jorge Silva (jorgelmsilva@ufrrj.br) on 2022-07-27T16:56:46Z No. of bitstreams: 1 2019 - Wellington Oliveira da Cruz.pdf: 14172587 bytes, checksum: 12767101c3271533d8d58b1826cc3777 (MD5)Made available in DSpace on 2022-07-27T16:56:47Z (GMT). No. of bitstreams: 1 2019 - Wellington Oliveira da Cruz.pdf: 14172587 bytes, checksum: 12767101c3271533d8d58b1826cc3777 (MD5) Previous issue date: 2019-08-06CAPES - Coordena??o de Aperfei?oamento de Pessoal de N?vel Superiorapplication/pdfhttps://tede.ufrrj.br/retrieve/70053/2019%20-%20Wellington%20Oliveira%20da%20Cruz.pdf.jpgporUniversidade Federal Rural do Rio de JaneiroPrograma de P?s-Gradua??o em Qu?micaUFRRJBrasilInstituto de Qu?micaAHMAD, Z.; SALEEMUDDIN, M.; SIDDI, M. Purification and characterization of three alkaline proteases from the gut of the larva of army worm, Spodoptera litura. Insect Biochemistry, v. 10, n. 6, p. 667?673, 1980. AHMEDANI, M. S.; HAQUE, M. I.; AFZAL, S. N.; ASLAM, M.; NAZ, S. Varietal changes in nutritional composition of wheat kernel (Triticum aestivum L.) caused by khapra beetle infestation. Pak. J. Bot. 41 (3), pp: 1511-1519. 2009. ALARC?N F. J.; MART?NEZ, T. F.; BARRANCO, P. 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Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor. Insect Molecular Biology, v. 12, n. 2, p. 135?145, 2003. ZHU, Y. C.; BAKER, J. E. Characterization of midgut trypsin-like enzymes and three trypsinogen cDNAs from the lesser grain borer, Rhyzopertha dominica (Coleoptera: Bostrichidae). Insect biochemistry and molecular biology,29(12), 1053-1063, 1999. ZINKLER, D.; POLZER, M. Identification and characterization of digestive proteinases from the firebrat thermobia domestica. 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dc.title.por.fl_str_mv Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
dc.title.alternative.eng.fl_str_mv Biochemical caracterization of digestive proteases in Alphitobius diaperinus (Coleoptera: Tenebrionidae) larvae
title Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
spellingShingle Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
Cruz, Wellington Oliveira da
Inseto
Dietas
Proteases
Alphitobius diaperinus
Insect
Diets
Proteases
Qu?mica
title_short Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
title_full Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
title_fullStr Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
title_full_unstemmed Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
title_sort Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae)
author Cruz, Wellington Oliveira da
author_facet Cruz, Wellington Oliveira da
author_role author
dc.contributor.advisor1.fl_str_mv Pontes, Emerson Guedes
dc.contributor.advisor1ID.fl_str_mv 045.534.107-96
dc.contributor.referee1.fl_str_mv Pontes, Emerson Guedes
dc.contributor.referee2.fl_str_mv Souza, Cristiane Martins de
dc.contributor.referee3.fl_str_mv Santos, Danielle M. P. de Oliveira
dc.contributor.referee4.fl_str_mv Mesquita, Rafael Dias
dc.contributor.referee5.fl_str_mv Sant`Anna, Carlos Mauricio
dc.contributor.authorID.fl_str_mv 075.736.047-50
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/5335761763028967
dc.contributor.author.fl_str_mv Cruz, Wellington Oliveira da
contributor_str_mv Pontes, Emerson Guedes
Pontes, Emerson Guedes
Souza, Cristiane Martins de
Santos, Danielle M. P. de Oliveira
Mesquita, Rafael Dias
Sant`Anna, Carlos Mauricio
dc.subject.por.fl_str_mv Inseto
Dietas
Proteases
Alphitobius diaperinus
topic Inseto
Dietas
Proteases
Alphitobius diaperinus
Insect
Diets
Proteases
Qu?mica
dc.subject.eng.fl_str_mv Insect
Diets
Proteases
dc.subject.cnpq.fl_str_mv Qu?mica
description Alphitobius diaperinus is considered an important issue in the avian environment. Studying your behavior, eating habits and digestive enzymes may indicate important targets in your control. Control of A. diaperinus is considered difficult, its natural enemies are little known, and the use of chemical insecticides is the main method of control. Insect digestive proteases catalyze the production of peptides and amino acids from a protein diet and they are found in the midgut region of insects. Proteolytic activities in the digestive tract of A. diper?nus larvae and adults were determined using azocasein and specific substrates after feeding on different diets. The crude extract of the digestive tract of A. diaperinus larvae showed activity on azocasein and Abz-Phe-Arg-MCA. It was inhibited by more than 50% by E-64 and activated by 2.0 mM DTT at acid pH. Nine bands were detected with proteolytic activity and molecular mass in the range 10 kDa - 100 kDa through zymogram, using 0.1% gelatin as substrate. Different classes of proteases were identified in the presence of classical protease inhibitors such as E-64, iodoacetamide and iodoacetic acid, PMSF, SBTI, aprotinin and TLCK. A higher level of proteolytic activity was observed at pHs between 5 and 6. Although combinations of serine and cysteine proteases have been observed, acid proteases showed higher levels of proteolytic activity. Calcium ion increased the protease activity at concentrations greater than 2.0 mM. Two-dimensional nano-HPLC and ESI-MS / MS analyzes resulted in the identification of proteases such as tripine, cathepsins, metalloproteases, aminopeptidases, peptidases and dipeptidases. High inhibitory potential of different series of imidazolone on cysteine protease was observed, what can be used as control tools of A. diaperinus.
publishDate 2019
dc.date.issued.fl_str_mv 2019-08-06
dc.date.accessioned.fl_str_mv 2022-07-27T16:56:47Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/doctoralThesis
format doctoralThesis
status_str publishedVersion
dc.identifier.citation.fl_str_mv CRUZ, Wellington Oliveira. Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae). 2019. 168 f. Tese (Doutorado em Qu?mica) - Instituto de Qu?mica, Universidade Federal Rural do Rio de Janeiro, Serop?dica, 2019.
dc.identifier.uri.fl_str_mv https://tede.ufrrj.br/jspui/handle/jspui/5822
identifier_str_mv CRUZ, Wellington Oliveira. Caracteriza??o bioqu?mica de proteases digestivas em larvas de Alphitobius diaperinus (Coleoptera: Tenebrionidae). 2019. 168 f. Tese (Doutorado em Qu?mica) - Instituto de Qu?mica, Universidade Federal Rural do Rio de Janeiro, Serop?dica, 2019.
url https://tede.ufrrj.br/jspui/handle/jspui/5822
dc.language.iso.fl_str_mv por
language por
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