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Universidade Federal Do Ceará Centro De Ciências Agrárias Departamento De Fitotecnia Programa De Pós-Graduação Em Agronomia/Fitotecnia

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Universidade Federal Do Ceará Centro De Ciências Agrárias Departamento De Fitotecnia Programa De Pós-Graduação Em Agronomia/Fitotecnia UNIVERSIDADE FEDERAL DO CEARÁ CENTRO DE CIÊNCIAS AGRÁRIAS DEPARTAMENTO DE FITOTECNIA PROGRAMA DE PÓS-GRADUAÇÃO EM AGRONOMIA/FITOTECNIA DOMINGOS FERREIRA DE MÉLO NETO ANÁLISE PROTEÔMICA DE SEMENTES EM DESENVOLVIMENTO DE AÇAÍ (Euterpe oleracea Mart.) FORTALEZA 2018 DOMINGOS FERREIRA DE MÉLO NETO ANÁLISE PROTEÔMICA DE SEMENTES EM DESENVOLVIMENTO DE AÇAÍ (Euterpe oleracea Mart.) Dissertação apresentada ao Programa de Pós- Graduação em Agronomia/Fitotecnia da UFC, como parte dos requisitos para obtenção do título de Mestre em Agronomia/Fitotecnia. Área de concentração: Fisiologia, Bioquímica e Biotecnologia Vegetal. Orientador: Prof. Francisco de Assis de Paiva Campos Coorientador: Prof. Fábio César Sousa Nogueira FORTALEZA 2018 DOMINGOS FERREIRA DE MÉLO NETO ANÁLISE PROTEÔMICA DE SEMENTES EM DESENVOLVIMENTO DE AÇAÍ (Euterpe oleracea Mart.) Dissertação apresentada ao Programa de Pós- Graduação em Agronomia/Fitotecnia da UFC, como parte dos requisitos para obtenção do título de Mestre em Agronomia/Fitotecnia. Área de concentração: Fisiologia, Bioquímica e Biotecnologia Vegetal. Aprovada em: 29/03/ 2018. BANCA EXAMINADORA _____________________________________________ Prof. Francisco de Assis de Paiva Campos (Orientador) Departamento de Bioquímica e Biologia Molecular Universidade Federal do Ceará (UFC) _____________________________________________ Prof. Fábio César Sousa Nogueira (Coorientador) Instituto de Química (IQ) Universidade Federal do Rio de Janeiro (UFRJ) _____________________________________________ Dra. Emanoella Lima Soares Plant Genetics Department University of Liège, Belgium Aos meus pais, Vanaldi e Lourinaldo, a minha irmã Alaídes Priscila, e a minha avó Alaíde! AGRADECIMENTOS À Deus pela Vida. Ao professor Francisco A. P. Campos pela oportunidade de realizar esse curso de mestrado sob sua orientação, pelos ensinamentos, treinamento e confiança. Ao professor Fábio C. S. Nogueira pela disponibilidade em participar da avaliação desse trabalho e, sobretudo pelo treinamento em espectrometria de massas e proteômica. A Dra Emanoella L. Soares (Manu) pela disponibilidade em participar da avaliação desse trabalho, como também pelas orientações e ajuda na definição e coleta dos frutos utilizados nesse estudo. Ao professor Gilberto B. Domont pela receptividade e por todo entusiasmo com a proteômica. À professora Rosilene Mesquita pelas contribuições no projeto de qualificação. Ao Fabiano pelas contribuições no projeto de qualificação e revisão dos textos dessa dissertação, além da amizade. Aos integrantes do Laboratório de Biologia Molecular de Plantas, João, Magda, Jessica, Thais e Evanildo, pelo companheirismo e ajuda no processamento do material vegetal. Ao Moab, meu amigo desde a graduação, o qual tive a honra de compartilhar praticamente todos os momentos ao longo desse curso de mestrado. Ao Roberto, por ter sido desde o início bastante atencioso, tanto nas orientações laboratorias, como pela ajuda nas disciplinas e, sobretudo, pela amizade construída. A Raquel por ter sido uma verdadeira guia nos experimentos na Unidade Proteômica. Ao Daniel, também meu amigo desde a gradução, um cara que admiro muito. Ao Sr. Erivan pela ajuda na coleta dos frutos. Ao pessoal dos laboratórios de Defesa de Plantas e Toxinas Vegetais da UFC, Lucas, Helen, Thiago, Del e Raissa pela ajuda na liofilização dos frutos. Ao pessoal do Laboratório de Fisiologia Vegetal da UFC, Ana Carla, Fabrício e Elieser, por também ajudarem na liofilização dos frutos e fornecerem inibidor de protease. Aos integrantes da Unidade Proteômica do Instituto de Química da UFRJ, Prof. Magno, Natália, Larissa, Vinícius, Yara, Michely, Mariana, Isis, Liege, Simone, Lidiane, Renata, Ana Beatriz, Rafael, em especial a Erika. Aos professores do curso de Pós-Graduação em Agronomia/Fitotecnia. Aos meus pais, Vanaldi e Lourinaldo, e a minha irmã Alaídes, por todo amor, carinho, confiança e, sobretudo pela base educacional que me deram. À minha namorada Aisla pelo amor, carinho, paciência e palavras de conforto nos momentos mais difíceis desse curso. Aos órgãos e instituições financiadores dessa pesquisa: CNPq, UFC e UFRJ A todos que de alguma maneira contribuíram na realização desse trabalho. RESUMO O açaí (Euterpe oleracea Mart) pertence à família Arecaceae e sua importância econômica está centrada basicamente na colheita do fruto para produção de polpa. Nos últimos anos, a demanda pela polpa de açaí aumentou de forma significativa, em função principalmente do apelo funcional. No entanto, a maior parte da colheita corresponde à semente (caroço), normalmente descartada como resíduo durante o processo produtivo, não havendo, pois, alternativas viáveis para o seu aproveitamento em larga escala. Diante desse problema, entende-se que estudos básicos, possam fornecer subsídios capazes de melhor direcionar sua utilização. Nessa perspectiva, realizou-se uma análise proteômica livre de marcação de sementes de E. oleracea em quatro estádios de desenvolvimento, designados E3, E6, E9 e E11, o que resultou na identificação de 758, 897, 285 e 69 proteínas, respectivamente, e um total de 1.080 proteínas. A categorização funcional dessas proteínas nos mostrou que a maioria integra as classes de metabolismo de carboidrato, metabolismo de aminoácidos, síntese de proteínas, parede celular, metabolismo secundário, metabolismo de lipídeos, transportadores e metabolismo de EROS. Já, na quantificação relativa, realizada com base na intensidade do íon precursor, foram identificadas 21, 43, 14, 37, 14 e 3 proteínas diferencialmente expressas pelo teste t (p ˂ 0,05), nos contrastes E6/E3, E9/E3, E11/E3, E9/E6, E11/E6 e E11/E9, respectivamente. As proteínas com padrão de expressão semelhante foram agrupadas em seis grupos distintos. A abundância relativa das enzimas sacarose sintase, UTP-glucose-1-fosfato-uridilitransferase, α-galactosidase, manose-1-fosfato- guanililtranferase e peroxidase 72 foi aumentada no E6, sugerindo que nessa fase do desenvolvimento, ocorrem simultaneamente os processos de deposição e modificação dos polissacarídeos da parede celular e, indica a formação de polissacarídeos a base de manose, que devem constituir a fração hemicelulósica. Proteínas de reserva do tipo globulina 63 KDa e globulina 7S foram acumuladas até a maturidade, a partir do E6. Essa análise proteômica de sementes em desenvolvimento de açaí, focou alguns aspectos da formação das paredes celulares, ja que essas são o principal repositório de substâncias de reserva nas sementes dessa espécie, como também, trata das principais proteínas de armazenamento, de modo a fornecer conhecimento básico que ajude a melhor direcionar a utilização da semente de açaí. Palavras-chave: Euterpe oleracea. Formação de semente. Paredes celulares. Proteínas de armazenamento. Proteoma. ABSTRACT Açaí (Euterpe oleracea Mart) belongs to the family Arecaceae and its economic importance is centered mainly on fruit harvesting for pulp production. In recent years, the demand for açaí pulp increased significantly, mainly due to the functional appeal. However, most of the harvest corresponds to the seed, normally discarded as waste during the production process, once there are no viable alternatives for its use on a large scale. Considering such problem, it is understood that basic studies, can provide subsidies capable of improving seed use. In this perspective, a label-free proteomic analysis of E. oleracea seed was carried out at four developmental stages, designated E3, E6, E9 and E11, which resulted in the identification of 758, 897, 285 and 69 proteins respectively, and a total of 1,080 proteins. The functional categorization of these proteins, showed that most of them integrated the classes of carbohydrate metabolism, amino acid metabolism, protein synthesis, cell wall, secondary metabolism, lipid metabolism, transporters and EROS metabolism. Already, in the relative quantification using precursor ion intensity, 21, 43, 14, 37, 14 and 3 proteins were identified as differentially expressed by the test t (p ˂ 0,05), in the contrasts E6/E3, E9/E3, E11/E3, E9/E6, E11/E6 and E11/E9, respectively. Proteins with similar expression pattern were grouped into six distinct groups. The relative abundance of the enzymes sucrose synthase, UTP-glucose-1- phosphate-uridyl transferase, α-galactosidase, mannose-1-phosphate guanyliltranferase and peroxidase 72 was increased at E6, suggesting that at this developmental stage both deposition and modification of cell wall polysaccharides and indicates the formation of polysaccharides based on mannose, which should constitute the hemicellulosic fraction. Storage proteins type 63 KDa globulin like protein and 7S globulin were accumulated in seed until maturity starting at E6. These proteomic analysis the seed in development of açaí, focusing on some aspects of cell wall formation, since it is the main repository of reserve substances in the seeds of this species, as well as the main storage proteins, in order to provide basic knowledge that helps to better target the use of the acai seed. Key words: Euterpe oleracea. Seed formation. Storage proteins. Cell wall. Proteome. LISTA DE FIGURAS Figura 1 - Euterpe oleracea Mart. (açaí do Pará). A - Imagem da palmeira multicaule E. oleracea Mart. B – Inflorescência tipo raque de E. oleracea localizada abaixo das folhas e com frutos maduros de coloração roxo púrpura. C – Fruto e semente de E. oleracea em corte transversal .................................... 16 Figura 2 - Importância econômica do açaí (Euterpe oleracea Mart.) no Brasil. A - Produção histórica anual
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