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dc.creatorSantos, Monique Barreto-
dc.creator.Latteshttp://lattes.cnpq.br/1122184213413791por
dc.contributor.advisor1Rojas, Edwin Elard Garcia-
dc.contributor.advisor1Latteshttp://lattes.cnpq.br/1205756654416987por
dc.contributor.referee1Souza, Clitor Junior Fernandes de-
dc.contributor.referee2Carvalho, Carlos Wanderlei Piler-
dc.date.accessioned2016-10-17T10:53:24Z-
dc.date.issued2016-02-29-
dc.identifier.citationSANTOS, Monique Barreto. Estudo da formação dos complexos coacervados obtidos a partir de proteínas globulares. 2016. 97 f. Dissertação (mestrado em CIÊNCIA E TECNOLOGIA DE ALIMENTOS). Instituto de Tecnologia, Universidade Federal Rural do Rio de Janeiro, Seropédica, RJ, 2016.por
dc.identifier.urihttps://tede.ufrrj.br/jspui/handle/jspui/1297-
dc.description.resumoProteínas são biopolímeros de grande importância nutricional e funcional tendo sido amplamente utilizadas como ingredientes alimentares. A interação entre duas proteínas diferentes e opostamente carregadas pode dar origem aos complexo coacervado, atualmente utilizados como ingrediente na tecnologia de alimentos ou como agente de microencapsulação. A formação de complexos coacervados entre Ovalbumina e Lisozima e entre Albumina sérica bovina (BSA) e Lisozima foi investigada em função do pH, razão de massa total e concentração de NaCl. Para as duas interações estudadas, a complexação acorreu em uma ampla faixa de pH, que corresponde ao intervalo entre os pI das proteínas. Entre Ovalbumina e Lisozima a interação foi mais intensa na razão r=1 em pH 7,5 e para BSA e Lisozima a maior formação de complexos ocorreu na razão r=0,5 e pH 9,0. Alterações na força iônica por adição de NaCl influenciaram negativamente a interação entre Albumina BSA e Lisozima já na concentração de 0,01 mol/L e a 0,03 mol/L suprimiu a interação entre Ovalbumina e Lisozima. Por meio do Potencial - zeta pode-se verificar que a formação de complexos insolúveis foi máxima próximo ao pI para todas as razões estudadas, indicando que a interação se deu por neutralização de cargas opostas. Os espectros no infravermelho sugeriram que interações eletrostáticas conduziram as interações no entanto, ligações de hidrogênio também tiveram participação no processo de coacervação para as proteínas em estudo. As micrografias revelaram que os complexos insolúveis apresentavam estrutura esférica e o tamanho de partícula demonstrou a formação de estruturas com tamanho médio em torno de 2 m, as quais são bem maiores do que o tamanho obervado para as proteínas isoladas. A calorimetria de titulação isotérmica demonstrou que a interação entre Ovalbumina e Lisozima foi exotérmica, a qual ocorreu em duas etapas, a primeira entropicamente dirigida e a segunda entalpicamente dirigida. A calorimetria diferencial de varredura sugeriu, pela presença de um único ponto de desnaturação, que a interação entre BSA e Lisozima deu origem a um novo biopolímero com temperatura de desnaturação a 67°C, diferente das proteínas isoladas. Estes estudos sugeriram que complexos coacervados formados entre Ovalbumina / Lisozima e BSA / Lisozima poderiam ser utilizados como agente encapsulante de bioativos ou como ingredientes alimentares com o objetivo de agregar valor nutricional.por
dc.description.abstractProteins are biopolymers of high nutritional and functional significance has been widely used as food ingredients. The interaction between two different proteins oppositely charged, and can give rise to complex coacervate currently used as an ingredient in food technology or as a microencapsulating agent. The formation of complex coacervates between Lysozyme and Ovalbumin and between Bovine serum albumin (BSA) and Lysozyme has been investigated as a function of pH, mass ratio of total and concentration of NaCl. For both interactions studied, complexing latched in a wide pH range which corresponds to the interval between the pI of proteins. Among Ovalbumin and Lysozyme interaction was more intense in the ratio r = 1 at pH 7.5 and BSA and Lysozyme most complex formation has occurred on the ratio r = 0.5 and pH 9.0. Changes in the ionic strength by adding NaCl negatively affected the interaction between Lysozyme and BSA already at a concentration of 0.01 mol / L and 0.03 mol / L abolished the interaction between Lysozyme and Ovalbumin. Through Potential - zeta can be seen that the formation of insoluble complexes was highest near the pI for all studied reasons, indicating that the interaction is given by neutralization of opposite charges. The Infrared spectra suggested that electrostatic interactions led interactions however, hydrogen bonds also had a hand in the coacervation process for the proteins under study. The micrographs showed that the insoluble complexes showed spherical structure and particle size showed the formation of structures with an average size around 2 m, much larger than the observable size for the isolated proteins. The isothermal titration calorimetry showed that the interaction between Lysozyme and Ovalbumin was exothermic and was performed in two steps, the first and second entropy directed enthalpy driven. The differential scanning calorimetry suggested the presence of a single point of denaturation, that the interaction between Lysozyme and BSA led to a new biopolymer with denaturation temperature 67 ° C differs from isolated proteins. These studies suggested that complex coacervates formed between Ovalbumin / Lysozyme and BSA / Lysozyme could be used as the encapsulating bioactive agent or as food ingredients in order to add nutritional value.eng
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dc.description.provenanceMade available in DSpace on 2016-10-17T10:53:24Z (GMT). No. of bitstreams: 1 2016 - Monique Barreto Santos.pdf: 2356049 bytes, checksum: 8a379b47682a5e067746503ee59b6d27 (MD5) Previous issue date: 2016-02-29eng
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico - CNPqpor
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dc.languageporpor
dc.publisherUniversidade Federal Rural do Rio de Janeiropor
dc.publisher.departmentInstituto de Tecnologiapor
dc.publisher.countryBrasilpor
dc.publisher.initialsUFRRJpor
dc.publisher.programPrograma de Pós-Graduação em Ciência e Tecnologia de Alimentospor
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dc.rightsAcesso Abertopor
dc.subjectMicroencapsulationeng
dc.subjectDifferential scanning calorimetryeng
dc.subjectMicroencapsulantepor
dc.subjectCalorimetria diferencial de varredurapor
dc.subjectCalorimetria de titulação isotérmicapor
dc.subjectIsothermal titration calorimetrypor
dc.subject.cnpqCiência e Tecnologia de Alimentospor
dc.titleEstudo da formação dos complexos coacervados obtidos a partir de proteínas globularespor
dc.title.alternativeStudy of formation of complex coacervates obtained from globular proteinseng
dc.typeDissertaçãopor
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