{"id":421,"date":"2019-01-25T18:36:19","date_gmt":"2019-01-25T20:36:19","guid":{"rendered":"http:\/\/sites.usp.br\/lbbp\/?page_id=421"},"modified":"2019-04-25T18:00:53","modified_gmt":"2019-04-25T20:00:53","slug":"gabriel","status":"publish","type":"page","link":"https:\/\/sites.usp.br\/lbbp\/gabriel\/","title":{"rendered":"Gabriel Stephani de Oliveira"},"content":{"rendered":"<p>Doutor pelo programa de P\u00f3s-gradua\u00e7\u00e3o Interunidades em Biotecnologia da Universidade de S\u00e3o Paulo (2018). Graduou-se em 2012 no curso de gest\u00e3o ambiental na Universidade de S\u00e3o Paulo, onde tamb\u00e9m realizou duas inicia\u00e7\u00f5es cient\u00edficas na \u00e1rea de Biologia molecular e Biotecnologia com bolsa CNPq.<\/p>\n<p>N\u00b0 USP:6414660<\/p>\n<p>E-mail USP: gabriel.stephani.oliveira@usp.br<\/p>\n<p>N\u00b0 ORCID: <a href=\"https:\/\/nam04.safelinks.protection.outlook.com\/?url=https%3A%2F%2Forcid.org%2F0000-0002-9261-0310&amp;data=02%7C01%7C%7C77b4ca68a5ca40d9dcb208d56f00e155%7C84df9e7fe9f640afb435aaaaaaaaaaaa%7C1%7C0%7C636536971929346496&amp;sdata=KWjebAz%2FlyGYDeuXM75D5C2rM6oIqIc9PwkJ%2BW0Y5NI%3D&amp;reserved=0\">0000-0002-9261-0310<\/a><\/p>\n<p><a href=\"http:\/\/lattes.cnpq.br\/8806492346654313\">Link CV Lattes<\/a><\/p>\n<p><strong>Forma\u00e7\u00e3o<\/strong><\/p>\n<p>1- Gradua\u00e7\u00e3o: Bacharelado em Gest\u00e3o Ambiental<\/p>\n<p>Data de conclus\u00e3o: 30\/11\/2012<\/p>\n<p>IES: Escola de Artes, Ci\u00eancias e Humanidades da Universidade de S\u00e3o Paulo<\/p>\n<p>2- P\u00f3s-gradua\u00e7\u00e3o<\/p>\n<p>&#8211; N\u00edvel Doutorado Direto<\/p>\n<p>Curso: Programa de P\u00f3s-Gradua\u00e7\u00e3o Interunidades em Biotecnologia<\/p>\n<p>Ano de ingresso: 2013<\/p>\n<p>Projeto: Clonagem e caracteriza\u00e7\u00e3o da enzima ep\u00f3xido hidrolase de <em>Trichoderma reesei<\/em><\/p>\n<p><strong>Resumo:<\/strong><\/p>\n<p>Ep\u00f3xido hidrolases (EHs) s\u00e3o enzimas que catalisam a hidr\u00f3lise de ep\u00f3xidos a seus correspondentes di\u00f3is, apresentam potencial aplica\u00e7\u00e3o biotecnol\u00f3gica (separa\u00e7\u00e3o de enanti\u00f4meros na produ\u00e7\u00e3o de f\u00e1rmacos), est\u00e3o envolvidas no metabolismo de \u00e1cidos graxos poliinsaturados e inibidores de EHs est\u00e3o sendo estudados para poss\u00edvel utiliza\u00e7\u00e3o no tratamento de doen\u00e7as. Uma enzima ep\u00f3xido hidrolase (TrEH) do fungo filamentoso Trichoderma reesei QM9414 foi clonada, expressa, purificada e caracterizada funcionalmente e estruturalmente. A atividade de TrEH foi determinada com o substrato \u00f3xido de estireno (rac\u00eamico), demonstrando maior atividade nas temperaturas de 23 a 50 \u00b0C, no pH 7,2 a 37 \u00baC, e as constantes cataliticas Km= 4,6 mM e kcat= 336 s-1. A enzima recombinante mostrou ser enantiosseletiva, pois hidrolisa preferencialmente (S)-(-)-\u00f3xido de estireno, (R)-(-)-epicloridrina e (S)-(-)-1,2-epoxibutano. Mol\u00e9culas inibidoras da atividade de TrEH foram identificadas e algumas delas inibem at\u00e9 60% o crescimento de T. reesei. A estrutura terci\u00e1ria de TrEH (1,7 \u00c5) foi determinada por cristalografia, apresenta dobramento \u03b1\/\u03b2-hidrolase e n\u00e3o tem alta homologia com nenhuma outra estrutura de EH. TrEH \u00e9 uma nova enzima ep\u00f3xido hidrolase sol\u00favel cujas propriedades mostram seu potencial de utiliza\u00e7\u00e3o em aplica\u00e7\u00f5es biotecnol\u00f3gicas.<\/p>\n<p>Bolsa Agencia: FAPESP<\/p>\n<p>Processo: 2015\/03329-9<\/p>\n<p>Vig\u00eancia: Outubro 2015 \u2013 Maio 2018<\/p>\n<p><strong>Publica\u00e7\u00f5es:<\/strong><\/p>\n<p><strong>Artigos em peri\u00f3dicos cient\u00edficos:<\/strong><\/p>\n<ol>\n<li>de Oliveira GS, Adriani PP, Ribeiro JA, Morisseau C, Hammock BD, Dias MVB, Chambergo FS. The molecular structure of an epoxide hydrolase from Trichoderma reesei in complex with urea or amide-based inhibitors. Int J Biol Macromol. 2019 Feb 13;129:653-658. doi: 10.1016\/j.ijbiomac.2019.02.070.<\/li>\n<li>de Oliveira GS; Adriani PP; Wu H; Morisseau C; Hammock BD; Chambergo, FS. Substrate and inhibitor selectivity, and biological activity of an epoxide hydrolase from Trichoderma reesei. Mol Biol Rep. 2018 Nov 13. doi: 10.1007\/s11033-018-4481-4.<\/li>\n<li>Wilson, C., De Oliveira, G. S., Adriani, P. P., Chambergo, F. S., Dias, M. V. (2017). Structure of a soluble epoxide hydrolase identified in Trichoderma reesei. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1865(8), 1039-1045.<\/li>\n<li>de Oliveira, G. S., Adriani, P. P., Borges, F. G., Lopes, A. R., Campana, P. T., Chambergo, F. S. (2016). Data set of optimal parameters for colorimetric red assay of epoxide hydrolase activity. Data in brief, 8, 436-440.<\/li>\n<li>de Oliveira, G. S., Adriani, P. P., Borges, F. G., Lopes, A. R., Campana, P. T., Chambergo, F. S. (2016). Epoxide hydrolase of Trichoderma reesei: biochemical properties and conformational characterization. International journal of biological macromolecules, 89, 569-574.<\/li>\n<\/ol>\n<p><strong>Cap\u00edtulos de livros publicados:<\/strong><\/p>\n<ol>\n<li>Chambergo, F. S., Borges, F. G., Adriani, P. P., De Oliveira, G. S., Valencia, E. Y., Prasad, R. (2015). Biomass and Bioenergy. In: Ram Prasad; Sri Sivakumar; Umesh Chandra Sharma. (Org.). Bioenergy. 1ed. Studium Press LLC, USA.<\/li>\n<\/ol>\n<p>&nbsp;<\/p>\n<p><strong>Participa\u00e7\u00e3o em eventos:<\/strong><\/p>\n<ol>\n<li>de Oliveira, G. S., Adriani, P.P., Morissau, C., Hammock, Chambergo, F. S. (2018). Identification and characterization of inhibitors of epoxide hydrolase from Trichoderma reesei. In: 20th International Conference on Biotechnology, Biomechanics and Synthetic Biology (ICBBSB 2018) Sydney, Australia.<\/li>\n<li>de Oliveira, G. S., Adriani, P.P., Chambergo, F. S. (2017). Enantioselective hydrolysis of styrene oxide with epoxide hydrolase from the fungus Trichoderma reesei. In: 46th Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology (SBBq).<\/li>\n<li>de Oliveira, G. S., Adriani, P. P., Lopes, A. R., Campana, P. T., Chambergo, F. S. (2016). Epoxide hydrolase from the fungus Trichoderma reesei: Biochemical porperties and conformational characterization. In: 45th Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology (SBBq).<\/li>\n<li>de Oliveira, G. S., Chambergo, F. S. (2015). Enantioselectivity of the epoxide hydrolase enzyme from Trichoderma reesei. In: 23rd International Congress of the IUBMB and 44th Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology (SBBq).<\/li>\n<li>de Oliveira, G. S., Ignacio, M., Chambergo, F. S. (2014). Epoxide hydrolases enzymes from Trichoderma reesei. In: 43th Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology.<\/li>\n<li>de Oliveira, G. S., Chambergo, F. S. (2012). Promoter analysis of the gene encoding the pyruvate decarboxylase enzyme from Trichoderma reesei. In: 41th Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society.<\/li>\n<li>de Oliveira, G. S., Villela, L. C., Bernardes, M. L., Chambergo, F. S. (2011). Cellobiohydrolase I production on glucose-containing media by Saccharomyces cerevisiae. In: 40th Annual Meeting of Brazilian Biochemistry and Molecvular Biology Society.<\/li>\n<li>de Oliveira, G. S., Villela, Campana, P. T., ., Chambergo, F. S. (2010). Cloning, expression and purification of heterologous nitrilase 1 enzyme from Trichoderma reesei. In: VI Congresso brasileiro de Micologia.<\/li>\n<\/ol>\n","protected":false},"excerpt":{"rendered":"<p>Doutor pelo programa de P\u00f3s-gradua\u00e7\u00e3o Interunidades em Biotecnologia da Universidade de S\u00e3o Paulo (2018). Graduou-se em 2012 no curso de gest\u00e3o ambiental na Universidade de S\u00e3o Paulo, onde tamb\u00e9m realizou duas inicia\u00e7\u00f5es cient\u00edficas na \u00e1rea de Biologia molecular e Biotecnologia com bolsa CNPq. N\u00b0 USP:6414660 E-mail USP: gabriel.stephani.oliveira@usp.br N\u00b0 ORCID: 0000-0002-9261-0310 Link CV Lattes Forma\u00e7\u00e3o<a href=\"https:\/\/sites.usp.br\/lbbp\/gabriel\/\">[&#8230;]<\/a><\/p>\n","protected":false},"author":208,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_monsterinsights_skip_tracking":false,"_monsterinsights_sitenote_active":false,"_monsterinsights_sitenote_note":"","_monsterinsights_sitenote_category":0,"footnotes":"","_links_to":"","_links_to_target":""},"class_list":["post-421","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/pages\/421","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/users\/208"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/comments?post=421"}],"version-history":[{"count":2,"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/pages\/421\/revisions"}],"predecessor-version":[{"id":1024,"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/pages\/421\/revisions\/1024"}],"wp:attachment":[{"href":"https:\/\/sites.usp.br\/lbbp\/wp-json\/wp\/v2\/media?parent=421"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}