Mostrar registro simples

dc.creatorGomes, Daniela Silva
dc.date.accessioned2017-06-01T18:20:39Z
dc.date.accessioned2023-03-22T17:28:11Z
dc.date.available2013-09-16
dc.date.available2023-03-22T17:28:11Z
dc.date.issued2013-02-27
dc.identifier.citationGOMES, Daniela Silva. Produção de cutinases por Escherichia coli recombinante e potencial para aplicação ambiental. 2013. 88 f. Dissertação (Mestrado em Desenvolvimento de Processos Ambientais) - Universidade Católica de Pernambuco, Recife, 2013.por
dc.identifier.urihttps://hdl.handle.net/20.500.12032/76160
dc.description.abstractCutinase (EC 3.1.1.74) are enzymes that catalyze the hydrolysis of cutin, an insoluble biopolyester that compound the cuticle of plants. These enzymes have potential in the synthesis of triglycerides, polymers, surfactants in chemical, pharmaceutical and agrochemical industries. Cutinases have been applied to the surface modification of polymers, facilitating the degradation of these compounds. The aim of this work was to produce and characterize cutinases by Escherichia coli genetically engineered for use in the treatment of polyethylene terephthalate (PET). E. coli CUT and E. coli CUT-N1 were grown in Lysogeny broth (LB) in the presence of 100 μg/ml ampicillin and isopropyl β-D-1-tiogalactopiranosídeo (IPTG) as inducer. Cutinases activities were determined in the presence of p-nitrophenyl butyrate (p- NPB). The maximum cutinase activity was 1.4 U/mL, determined in the cell-free metabolicliquid, produced by E. coli CUT-N1. The metabolic liquid with activity of cutinase produced by E. coli CUT and E. coli CUT-N1 were concentrated two times by ultrafiltration and formulated with microbial preservatives and stabilizing substances of protein structures. Cutinases had optimum pH equal to 7.0 and thermal stability at 30 - 50 °C. The addition of (NH4)2SO4 at concentrations less than 10% stabilized cutinase activity for 60 days at 28 °C. Cutinases produced by cultures of E. coli degraded the plastic polyethylene terephthalate (PET) with a weight loss of 0.90%. Recombinant microbial cutinases are an alternative for application in biological treatment of plastics.eng
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico
dc.formatapplication/pdfpor
dc.languageporpor
dc.publisherUniversidade Católica de Pernambucopor
dc.rightsAcesso Abertopor
dc.subjectescherichia colipor
dc.subjectcutinasepor
dc.subjectbiotecnologiapor
dc.subjectdissertaçõespor
dc.subjectEscherichia colieng
dc.subjectcutinaseeng
dc.subjectbiotechnologyeng
dc.subjectdissertationseng
dc.titleProdução de cutinases por Escherichia coli recombinante e potencial para aplicação ambientalpor
dc.typeDissertaçãopor


Arquivos deste item

ArquivosTamanhoFormatoVisualização
daniela_silva_gomes.pdf1.405Mbapplication/pdfVisualizar/Abrir

Este item aparece na(s) seguinte(s) coleção(s)

Mostrar registro simples


© AUSJAL 2022

Asociación de Universidades Confiadas a la Compañía de Jesús en América Latina, AUSJAL
Av. Santa Teresa de Jesús Edif. Cerpe, Piso 2, Oficina AUSJAL Urb.
La Castellana, Chacao (1060) Caracas - Venezuela
Tel/Fax (+58-212)-266-13-41 /(+58-212)-266-85-62

Nuestras redes sociales

facebook Facebook

twitter Twitter

youtube Youtube

Asociaciones Jesuitas en el mundo
Ausjal en el mundo AJCU AUSJAL JESAM JCEP JCS JCAP