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dc.contributor.authorFontoura, Laís Martins
dc.date.accessioned2023-12-22T01:47:05Z-
dc.date.available2023-12-22T01:47:05Z-
dc.date.issued2013-08-23
dc.identifier.citationFONTOURA, Laís Martins. Efeito da alta pressão hidrostática sobre o colágeno da carne bovina. 2013. 61 f. Dissertação (Mestrado em Ciência e Tecnologia de Alimentos) - Instituto de Tecnologia, Universidade Federal Rural do Rio de Janeiro, Seropédica, 2013.por
dc.identifier.urihttps://rima.ufrrj.br/jspui/handle/20.500.14407/11119-
dc.description.abstractA maciez, atributo de textura, é um dos aspectos mais importantes para a qualidade da carne. Existem muitos fatores que determinam a maciez da carne, como os físico-químicos, enzimáticos, espécie do animal, raça, tipo de músculo e idade. Ainda é possível tornar a carne mais macia com diversos métodos como o uso de enzimas específicas, descarga elétrica, ultrassom e alta pressão hidrostática. As alterações de textura durante o processamento são resultantes de modificações estruturais. A aplicação da tecnologia de alta pressão hidrostática em carnes para o amaciamento ou maturação é dependente de fatores intrínsecos (determinados pela composição e fase do rigor-mortis) e das variáveis do processo: pressão, tempo e temperatura. Efeitos distintos decorrem de modificações da estrutura das proteínas, aumentando ou reduzindo a maciez de vários cortes cárneos, devido a possível fragmentação de proteínas miofibrilares e/ou enfraquecimento do tecido conjuntivo. As modificações no colágeno decorrentes dos processos podem ser determinadas pela quantificação da hidroxiprolina, um aminoácido em alta concentração e quase exclusivo do colágeno, incomum em outras proteínas. Objetivou-se com esse trabalho estudar as modificações no colágeno decorrentes da aplicação da alta pressão hidrostática na carne bovina. O músculo bovino foi pressurizado em 200, 400 e 600 MPa por 10 e 20 min. Extraíram-se os colágenos do perimísio e endomísio, que foram liofilizados. Foram realizadas análises do perfil das proteínas, solubilidade do colágeno, análise térmica por calorímetro diferencial de varredura e microscopia eletrônica de varredura. As modificações ocorridas no perimísio detectadas pela análise eletroforética foram mais evidentes em torno das bandas próximas de 103 kDa, representando as proteínas  da cadeia de colágeno, e nas bandas em torno de 180 kDa e 200kDa, que representam, respectivamente, a cadeia pesada da miosina e as proteínas  da cadeia de colágeno. Novas faixas de peptídeos foram observadas nos tratamentos em relação à amostra controle. Esse perfil pode ser consequência da mudança ocorrida no perimísio pela APH, bem como das alterações de proteínas miofibrilares e/ou sarcoplasmáticas. Pode-se concluir que a pressurização é capaz de aumentar as características do colágeno, tornando-o mais solúvel, com possível aumento na maciez da carne. Não foi possível concluir que houve alterações no perimísio pela análise de microscopia eletrônica de varredura. De acordo com o presente trabalho, pode-se concluir que a APH foi capaz de modificar a estrutura do colágeno do perimísio e endomísio.por
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPESpor
dc.formatapplication/pdf*
dc.languageporpor
dc.publisherUniversidade Federal Rural do Rio de Janeiropor
dc.rightsAcesso Abertopor
dc.subjectpressurizaçãopor
dc.subjecthidroxiprolinapor
dc.subjecttecido conjuntivopor
dc.subjectanálise eletroforéticapor
dc.subjectcromatografia líquidapor
dc.subjectpressurizationeng
dc.subjecthydroxiprolineeng
dc.subjectconjunctive tissueeng
dc.subjectliquid chromatographyeng
dc.subjectelectrophoretic analyseeng
dc.titleEfeitos da alta pressão hidrostática sobre o colágeno da carne bovinapor
dc.title.alternativeEffects of high hydrostatic pressure on beef collageneng
dc.typeDissertaçãopor
dc.description.abstractOtherSoftness is a texture attribute being regarded as one of the main factors related to meat quality. Several factors determine meat softness such as physic-chemicals, enzymatic, animal species, muscle type and animal age. In addition, it is possible to turn the meat softer by applying different methods as the use of specific enzymes, electro shocks, ultrasound and high hydrostatic press as shockwaves. Texture changes along the processes are due to structural changes. Application of high hydrostatic pressure for meat softening depends on intrinsic factors (associated to composition and rigor mortis stage) and processing variables: pressure, time and temperature. Distinct effects result from protein structure modifications by enhancing or decreasing different meat cut softening, due to possible myofibril protein fragmentation or by weakening conjunctive tissue. Changes in collagen from the proceedings may be determined by quantification of hydroxyproline, an amino acid in high concentration and almost exclusively in collagen, uncommon in other proteins. This research aimed at studying collagen modification resulting from the application of high pressure on bovine meat. The muscle was pressurised at 200, 400 and 600 MPa for 10 and 20 min. Endomysium and perimysium collagens were extracted and freeze-dried. The following analyses were carried out: protein profile, collagen solubility, thermal analyses by differential scanning calorimetry and electronic scanning microscopy. Modifications on perimysium detected by electrophoretic analysis were more evident around 103 kDa band, representing the  proteins of collagen chain, and on the bands around 180 kDa to 200 kDa, associated to the heavy myosin and  proteins of collagen chain. . New peptides bands were observed on the treatments samples in comparison to the control. Such a profile may result from the changes that happen on perimysium due to high hydrostatic pressure, as well as modifications on myofibril and sarcoplasmic proteins. It is possible to conclude that high-pressure application was able to affect collagen characteristics turning it more soluble, with a possible effect on meat softness. It was not possible to detect any perimysium change from the scanning electronic microscopy. In overall it was possible to conclude that hydrostatic high pressure was capable of changing both perimysium and endomysium portion of collageneng
dc.contributor.advisor1Rosenthal, Amauri
dc.contributor.advisor1ID025.072.978-40por
dc.contributor.advisor1Latteshttp://lattes.cnpq.br/1329532290735502por
dc.contributor.advisor-co1Mathias, Simone Pereira
dc.contributor.advisor-co1Latteshttp://lattes.cnpq.br/3876932417920038por
dc.contributor.referee1Cabral Neto, Otávio
dc.contributor.referee2Godoy, Ronoel Luiz de Oliveira
dc.creator.ID056.626.676-83por
dc.creator.Latteshttp://lattes.cnpq.br/0990986523534694por
dc.publisher.countryBrasilpor
dc.publisher.departmentInstituto de Tecnologiapor
dc.publisher.initialsUFRRJpor
dc.publisher.programPrograma de Pós-Graduação em Ciência e Tecnologia de Alimentospor
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