Traduzindo weird english: considerações sobre a tradução de Achy Obejas para The brief wondrous life of Oscar Wao

IX Congresso Brasileiro de Hispanistas realizado nos dias 22 a 25 agosto 2016É possível deixar claro em uma tradução literária para o espanhol que uma determinada palavra ou expressão já estava nessa língua no original em inglês? Como lidar como coloquialismos produzidos em contextos diaspóricos? E, como questão final; como manter o caráter híbrido de um texto bilíngue ao traduzilo para sua língua minoritária? O presente trabalho aborda tais questões analisando o caso específico da tradução de Achy Obejas para o espanhol do romance vencedor do Pulitzer The brief wondrous life of Oscar Wao escrito pelo autor dominicano Americano Junot Díaz e publicado em 2007. O romance, elaborado em um complexo processo de mudança constante de código chamado por Evelyn NienMing Ch'ien weird English estabelece constantes inclusões de gírias identificadas com a comunidade latina radicada nos Estados Unidos e com frequência apresenta frases que de algum modo se apropriam de aspectos gramaticais do espanhol. Esse exercício de pesquisa se interessa especialmente nas estratégias desenvolvidas pela tradutora com o objetivo de representar a hibridez da língua literária de Díaz. De fato, Obejas tenta manter essas características utilizando determinados tipos de compensações semânticas que tem por meta dar ao leitor a impressão de também estar em contato com um texto literário bilíngue. Para explorar essa hipótese, conceitos translinguismo e bilinguismo literário serão ferramentas úteis. Finalmente, já que o codeswitching não é apenas um fenômeno linguístico, mas também um fenômeno cultural, este trabalho pretende demonstrar a importância de uma abordagem póscolonial para o trabalho com traduções literárias para o espanhol de textos identificados com a comunidade latina produzidos em contextos diaspóricos para fazer jus a complexidade desses objetos culturaisUNILA­-UNIOEST

FACILIDADES E DIFICULDADES DO CONTROLE SOCIAL EM SAÚDE NO BRASIL PARA A GARANTIA DO ACESSO À SAÚDE ENQUANTO DIREITO: uma revisão integrativa

Segundo a Declaração dos Direitos Humanos todos nascem livres e iguais em dignidade e em direitos (ONU, 1948), desse modo instituiu a saúde como um dos seus direitos. No Brasil o direito a saúde passou a ser garantido a partir da Constituição Federal de 1988 (BRASIL, 1988), e para tanto criou o Sistema Único de Saúde (SUS) para atender toda a população brasileira através do acesso universal e igualitário aos serviços de saúde. O SUS trouxe a novidade da participação da sociedade nas discussões e deliberações acerca das políticas e ações de saúde. A participação popular na política de saúde, de acordo com Laurell (2016), tem sido muito importante para a formulação e implementação do SUS, mas tem enfrentado desafios e alcançado resultados positivos e negativos

Teorias de Camada Límite Atmosférica

Resum

Design of micro- and nanostructures from β-lactoglobulin under selected environmental conditions

The 19th Gums & Stabilisers for the Food Industry Conference: Hydrocolloid multifunctionalityBovine -lactoglobulin (-Lg) is a globular protein and the major component of whey proteins (ca. 50 % of its protein content). Besides the high nutritional value, the biological properties and resistance to proteolytic degradation in the stomach, its gelation capacity is particularly important allowing the formation of bio-based micro- and nanostructures (e.g. particles and hydrogels). -Lg when heated above a critical temperature (i.e. denaturation temperature: 76 ºC) undergoes conformational changes followed by subsequent protein-protein interactions. The order and rates of aggregation is highly dependent on the temperature, pH and protein concentration and can result in the formation of micro- and nanostructures with different properties and morphologies. The understanding of the kinetics of aggregation and of the combined effect of such environmental conditions is essential to design protein structures with the desired functionalities and applications. The objective of the present work was to understand the heat-induced aggregation of -Lg, affected by combined environmental conditions (various pH, heating temperature and protein concentrations) that lead to the formation of -Lg food-grade micro- and nanostructures. In this study, -Lg at various concentration (5, 10 and 15 mg·mL-1) was solubilized in 25 mM of sodium phosphate buffer at different pH values (3, 4, 6 and 7) and heated at different temperatures (60, 70 and 80 ºC) below and above the denaturation temperature of -Lg. Afterwards, the effect of aforementioned conditions on the -Lg micro- and nanostructures formation was evaluated in terms of their particle size and polydispersity index (PDI) by dynamic light scattering. -Lg nanostructures showed particle sizes below 50 nm when formed at pH 3 and 7 for -Lg concentrations of 5, 10 and 15 mg·mL-1 and heating temperatures of 60, 70 and 80 ºC, however displayed high PDI values ( 0.5). When the temperature of heating increased above the denaturation temperature of -Lg (i.e. 80 °C), the PDI values of the structures at pH 6 showed the lowest values ( 0.2), independent of the -Lg concentration used. At pH 4, it was possible to obtain structures at microscale (i.e. 3 µm) independent of the -Lg concentration and heating temperature of 70 and 80 °C. At this pH, which is relatively close to the isoelectric point of -Lg (i.e. 5.2), the net charge of proteins is ca. zero, so the protein structures tend to aggregate, thus showing higher size values. Therefore, protein aggregation mechanisms appear to be controlled by the environmental conditions applied; therefore, an understanding of the quantitative effect of these conditions is crucial for rational design of protein structures at micro or nanoscale with tailor-made functionalities.SFRH/BPD/80766/2011, Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq,Brasil) and to the Fundação para a Ciência e Tecnologia (FCT,Portugal), respectively. This study was supported by FCT under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE 2020 (POCI-01-0145-FEDER-006684) and BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte 2020-Programa Operacional Regional do Norteinfo:eu-repo/semantics/publishedVersio

β-Lg nano delivery systems: sustained release of riboflavin into food simulants under various temperatures

β-Lactoglobulin (β-Lg), the main protein fraction of whey proteins, can be used to encapsulate bioactive compounds due to its gelation capacity, which allows forming nanostructures, and their affinity to bind to a wide range of molecules. Riboflavin is an essential vitamin for human growth and wellbeing, having thus been studied as hydrophilic model compound. Its use in food products is still limited by several issues including photodegradation and low solubility in water. Riboflavin encapsulation may overcome these issues and possibly display a controlled release behavior. Food-grade -Lg nanostructures (-LgN) were developed at pH 6, at 80 °C for 15 min to encapsulate 0.105 mg mL-1 of riboflavin. Release kinetics of riboflavin from -LgN were assessed in hydrophilic (ethanol 10%) and hydrophobic (ethanol 50%) food stimulants (Commission Regulation EU No10/2011) at 4 and 25 C. Kinetic models considering both Fickian and Case II transport (Linear Superposition Model - LSM) were fitted to release kinetics data. The impact of release conditions on particle size and surface charge of nanostructures was performed by dynamic light scattering (DLS). The LSM model was the most suitable to describe the release kinetics, which is mainly governed by a relaxation mechanism. These results were in agreement with DLS observations, which showed a decrease on surface charge and an increase on particle size. -LgN were relaxed and weaker as a consequence of the riboflavin release until the equilibrium state was reached. It was observed that the contribution of relaxation to the release mechanisms increases with temperature. Riboflavin release kinetics on the hydrophobic food simulant provided a higher riboflavin retention when compared with the hydrophilic food simulant, independently of temperature. These observations indicate that food-grade -LgN may represent suitable means for controlled delivery of hydrophilic compounds in food applications, however, further information is needed to clarify the mechanisms which are involved in it.CNPqFCTCOMPETE 2020NORTE 2020info:eu-repo/semantics/publishedVersio

Stability of β-Lactoglobulin micro- and nanostructures under various environmental conditions

β-Lactoglobulin (-Lg) comprises about 50-55% of total proteins in bovine whey serum and it is its principal gelling agent. Heat-induced gelation of -Lg above denaturation temperature (i.e. 76 oC) leads to exposure of initially buried hydrophobic regions, followed by subsequent protein-protein interactions, which is a critical step to design micro- and nanostructures1. These bio-based structures can be a promising vehicle for encapsulation and controlled delivery of different bioactive compounds (e.g. antioxidants, vitamins). Nonetheless, developing successful delivery systems requires the assessment of the physicochemical stability of these structures under distinct environmental conditions2. In this sense, the present work aims at exploring the impact of several conditions such as pH, thermal processing, ionic strength and storage temperature on the physicochemical properties of -Lg micro- and nanostructures. For this purpose, food-grade micro- and nanostructures, previously optimized, were prepared as follows: -Lg powder (5 15 mg mL-1) was solubilized in sodium phosphate buffer at pH 6 and then heated at 80 °C for 15 min. Subsequently, the effect of pH (from 2 to 10) using 0.1 mol L- 1 NaOH and/or H3PO4; temperature (from 20 to 80 °C, with 5 oC increments); ionic strength (from 0 to 200 mmol L-1) by adding NaCl; and storage temperature (4 oC and 25 °C) on -Lg micro- and nanostructures stability were evaluated in terms of particle size, polydispersity index (PDI) and surface charge (S) changes by dynamic light scattering (DLS). For pH between 2 and 4, and 6 and 10, microstructures showed particle size values ranging from 202.4 nm to 252.6 nm (p 0.8). The surface charge of -Lg micro- and nanostructures changed from positive (ca. +18 mV) at pH 2, to negative (ca. 20 mV) at pH 10, with net charge close to zero at pH 5 (i.e. near the isoelectric point of -Lg). Regarding thermal stability, the particle size of micro- and nanostructures remained constant and homogenous (i.e. PDI 0.05) between each condition tested. These findings provide new insights on which conditions the -Lg micro- and nanostructures are more stable, and therefore more suitable to act as potential delivery systems of bioactive compounds.CNPqFCTNORTE 2020COMPETE 2020info:eu-repo/semantics/publishedVersio

Bigels as a vehicle for bioactives compounds: assessment of in vitro digestion behavior

Bigels are novel complex biphasic systems composed by organic and aqueous gelled phases that can act as texture modifiers, and vehicle for topical and gastrointestinal delivery of hydrophilic/lipophilic bioactives. However, its behavior through digestion has still not been assessed. Moreover, process conditions can change their structure and consequently the bioactive stability and release. Thus, the aim of this work was to evaluate the influence of the process on bigels structure and behavior through gastrointestinal tract. Bigels were produced with gellan gum hydrogel (1.25% w/w) and high oleic sunflower oil+glycerol monostearate (10% w/w) organogel loaded with 0.1% curcumin. Gelling agents were solubilized separately (80 °C, 30 min) and then mixed by cold or hot-emulsification method. Cold-set was carried out mixing gelled systems by mechanical stirring (50 °C, 1,000 min-1, 10 min). Hot-emulsification was performed with addition of 2% (w/w) Tween 80 by mechanical stirring (same conditions) or rotor-stator device (50 °C, 14,000 min-1, 2 min). Bigels were submitted to an in vitro gastrointestinal digestion using the harmonized digestion method, and changes were assessed through fluorescent microscopy. At the end of digestion, free fatty acids (FFA) released and bioaccessibility and stability of curcumin were determined. Cold-set bigels showed W/O structure while hot-emulsification led to W/O bigels with smaller droplets when rotor-stator was used. The results from the in vitro digestion indicated that all bigels were stable after stomach conditions, however, they destabilized during intestinal conditions. Besides, O/W bigels showed higher stability with less droplets coalescence, due to the surfactant presence. FFA and curcumin stability followed the same tendency, with higher values for O/W bigels. However, despite the higher stability, the effective bioavailability was similar for all bigels produced. Thus, independent of the structure and physical properties, bigels could be used for protection and oral delivery of hydrophobic bioactives and are promising systems for concomitant hydrophilic/hydrophobic loading.FCTCOMPETE 2020NORTE 2020This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2019 unit and BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020 - Programa Operacional Regional do Norte.info:eu-repo/semantics/publishedVersio