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Pesquisa : G02.130 [Categoria DeCS]
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Id: biblio-1132182
Autor: Almeida, Lariana Negrão Beraldo; Pietrobelli, Juliana Martins Teixeira Abreu; Lenzi, Giane Gonçalves; Santos, Onélia Aparecida Andreo.
Título: Degradation of Caffeine by Heterogeneous Photocatalysis Using ZnO with Fe and Ag
Fonte: Braz. arch. biol. technol;63:e20180614, 2020. tab, graf.
Idioma: en.
Resumo: Abstract The organic compound caffeine when detected in environmental matrices such as surface waters and groundwater is considered as an emerging contaminant, in which its effects are still unknown. Therefore, in the present research, zinc oxide-based catalysts impregnated with iron and silver were prepared for the reaction of caffeine degradation by heterogeneous photocatalysis. The wet impregnation method with excess solvent was applied to the preparation of the materials, later they were characterized by adsorption of N2, X-ray diffraction and photoacoustic spectroscopy. Then, the photodegradation, photolysis and adsorption tests were carried out, in which it was observed that only the presence of the radiation or photocatalysts could not sufficiently degrade the caffeine, however when combined radiation with all the catalysts studied here presented degradation above 70% at the end of 300 minutes of the reaction, and the best catalyst studied was that containing 8% Ag in non-calcined ZnO. Thus, these results point out that the methodology employed in this research, both for the preparation of the catalysts and in the process of the photocatalysis reaction, was efficient in the degradation of the emerging contaminant, caffeine, which could later be used for a mixture of other contaminants.
Descritores: Prata/química
Óxido de Zinco/química
Cafeína/química
Catálise
Processos Fotoquímicos
-Adsorção
Reatores Biológicos
Ferro/química
Responsável: BR1.1 - BIREME


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Id: biblio-1132185
Autor: Castro, Luiz Eduardo Nochi de; Meurer, Eduardo César; Alves, Helton José; Santos, Marco Aurélio Reis dos; Vasques, Erika de Castro; Colpini, Leda Maria Saragiotto.
Título: Photocatalytic Degradation of Textile dye Orange-122 Via Electrospray Mass Spectrometry
Fonte: Braz. arch. biol. technol;63:e20180573, 2020. tab, graf.
Idioma: en.
Resumo: Abstract This work reports the study of the potential application of Zn/TiO2 catalysts, obtained by the sol-gel method, in processes of environmental decontamination through the reactions of photodegradation of textile dye, followed by electrospray mass spectrometry. The catalysts synthesis was performed according to a 2² factorial design with repetition at the central point. The characterization techniques used were: N2 adsorption measurements (BET method), scanning electron microscopy with energy dispersive X-ray (MEV/EDS), X-ray diffraction and point of zero charge (PZC). The photocatalytic tests were performed in batch in the presence of sunlight, and to evaluate the degradation kinetics study, a rapid direct injection electrospray mass spectrometry (DI-ESI-MS) method has been developed. By the photocatalytic tests, the calcination temperature of 400 °C has shown the best results of discoloration for the reactive Orange-122 dye (99.76%) in a reaction time of 2h. The discoloration kinetics were a pseudo-first order, and a statistical analysis was performed to investigate the effects of the variables and to optimize the conditions of discoloration to the dye. After the reactional time of 2 h, an ion of m/z 441.5 was detected by ESI-MS, indicating that the photocatalytic process was effective for the degradation of the dye to secondary compounds.
Descritores: Compostos Azo/toxicidade
Biodegradação Ambiental
Descontaminação/métodos
Espectrometria de Massas em Tandem/métodos
Recuperação e Remediação Ambiental/métodos
Águas Residuárias
-Fotoquímica
Têxteis/toxicidade
Microscopia Eletrônica de Varredura
Catálise
Domínio Catalítico
Espectrometria de Massas por Ionização por Electrospray
Corantes
Fotobiorreatores
Modelos Teóricos
Responsável: BR1.1 - BIREME


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Id: lil-499695
Autor: Guija poma, Emilio; Soberón, Mercedes; Haak Mares, Hielke.
Título: Mecanismo de acción de las fosfatasas ácidas de bajo peso molecular / Mechanism of action of low molecular weight acid phosphatases
Fonte: An. Fac. Med. (Perú);68(4):356-362, oct.-dic. 2007. tab, graf.
Idioma: es.
Resumo: Las fosfatasas ácidas son enzimas ampliamente distribuidas en la naturaleza y tienen la propiedad de hidrolizar fosfomonoésteres a pH 5,0, liberando como productos de la reacción un alcohol y fosfato inorgánico. Cuando se compara los valores de kcat/Km de las fosfatasas de hígado, de bovino, alpaca y porcino, nos permite sugerir que estas enzimas tienen elevada afinidad por el sustrato p-nitrofenil fosfato. Los productos que se liberan durante la catálisis por fosfatasa ácida, muestran que el fenol o el p-nitrofenol se comportan como inhibidores de tipo no competitivo, mientras que el fosfato inorgánico muestra una inhibición de tipo competitiva. Para evidenciar laprobable formación de un complejo covalente en la secuencia catalítica, se utilizó diversos nucleófilos más eficientes que el agua, tales como metanol, etanol y glicerol. Las modificaciones que produjeron en los valores Km, Vmax y los productos liberados en la reacción sugieren la formación de un complejo enzima-fosfato. El pH afecta los valores de Km y Vmax de las fosfatasas ácidas, un análisis del comportamiento de estas enzimas en un rango de pH comprendido entre 3,8 y 6,8 sugieren que en el sitio activo existe un residuo de aminoácido con un valor pKa de 6,0. El uso del dietilpirocarbonato, un compuesto que selectivamente reacciona con el residuo histidina en las proteínas, inhibe completamente a estas fosfatasas. Así mismo, un experimento de cinética de inhibición múltiple realizado en presencia de fosfato inorgánico y dietilpirocarbonato permite calcular un valor Ki que es igual al obtenido en otras condiciones experimentales. En tal sentido, las fosfatasas ácidas de bajo peso molecular catalizarían las reacciones a través de un modelo de tipo uni biordenado, con la formación de un complejo covalente intermedio, y que el residuo histidina participaría directamente en la catálisis.

Acid phosphatases are enzymes widespread in nature that hydrolyze phosphomonoesters at pH 5,0; this reaction yields alcohol and inorganic phosphate. Comparison of bovine, alpaca and porcine liver phosphatases kcat/Km values suggests these enzymes have a high affinity for p nitrophenyl phosphate substrate. Products that are released during acid phosphatase catalysis show that phenol or p nitrophenol behave as non competitive inhibitors, whereas inorganic phosphate shows competitive inhibition. Different nucleophiles more efficient than water have been used, such as methanol, ethanol and glycerol, showing the probable formation of a covalent complex in the catalytic sequence. Modifications produced in Km and Vmax values as well as in the reaction released products suggest the development of an enzyme-phosphate complex. pH affects acid phosphatases Km and Vmax values. Behavioral analysis of these enzymes at 3,8 to 6,8 pH range suggests the location of a pKa 6,0 aminoacid residue in the active site. The use of a diethylpyrocarbonate compound which selectively reacts with protein histidine residues completely inhibits this kind of phosphatases. Also, multiple inhibition kinetic survey performed in presence of inorganic phosphate and diethylpyrocarbonate allows a Ki value calculation equal to that obtained in other experimental conditions. In this respect, low molecular weight acid phosphatases would catalyze reactions through a uni biordered model, forming an intermediate covalent complex; histidine residues would directly participate in the catalysis.
Descritores: Catálise
Fosfatase Ácida
Mecanismos Moleculares de Ação Farmacológica
Responsável: PE1.1 - Oficina Universitária de Biblioteca


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Id: lil-499688
Autor: Guija Poma, Emilio; Arauco, Fernando; Soberón, Mercedes; Haak Mares, Hielke.
Título: Efecto del glicerol sobre la catálisis por fosfatasa ácida de bajo peso molecular de hígado de alpaca (lama pacos) / Effect of glycerol on catalysis by low molecular weight acid phosphatase from alpaca liver (lama pacos)
Fonte: An. Fac. Med. (Perú);68(4):307-313, oct.-dic. 2007. graf.
Idioma: es.
Resumo: Objetivo: Determinar el efecto del glicerol sobre la hidrólisis del p-nitrofenil fosfato a pH 5,0 por fosfatasa ácida de bajo peso molecular de hígado de alpaca. Diseño: Estudio analítico experimental. Lugar: Centro de Investigación de Bioquímica y Nutrición, Facultad de Medicina, Universidad Nacional Mayor de San Marcos. Materiales: Se utilizó los reactivos químicos p-nitrofenil fosfato sal disódica, ácido acético glacial, glicerol, ácido tricloroacético, ácido sulfúrico, molibdato de amonio, ácido ascórbico, sulfato de amonio, sephadex G-75 (45-120), sulfoetil sephadex C-50 y etilendiaminotetraacético (EDTA). Métodos: Se determinó los parámetros cinéticos Km y Vmax utilizando como sustrato el p-nitrofenil fosfato, en presencia de concentraciones variables de glicerol. Así mismo, se determinó la velocidad de liberación de los productos de la reacción en función de la concentración de dicho nucleófilo. Principales medidas de resultados: Efecto del glicerol sobre la hidrólisis del p-nitrofenil fosfato. Resultados: El glicerol en concentraciones comprendidas entre 1,16 y 3,49 M incrementó linealmente la liberación del p-nitrofenol; en cambio, la formación del fosfato inorgánico -el segundo producto liberado- no se modificó. Así mismo, los valores de Km y Vmax se incrementaron linealmente dependientes de las concentraciones de glicerol, en un rango comprendido entre 0,58 y 2,32 M. Conclusiones: Un análisis de las modificaciones que ejerce el glicerol sobre los valores de Km y Vmax y la velocidad de liberación de los productos de la reacción permite sugerir un modelo en el que la fosfatasa ácida de bajo peso molecular de hígado de alpaca cataliza la hidrólisis de fosfomonoésteres a través de un mecanismo uni biordenado, con la formación de un complejo enzima-fosfato, que sería escindido por agua o un nucleófilo, como el glicerol; en este modelo a k2 le corresponde un valor mucho mayor que k3 y k4 N.

Objective: To determine the effect of glycerol on hydrolysis of p-nitrophenyl phosphate at pH 5,0 by low molecular weight acid phosphatase from alpaca liver. Design: Experimental analytical study. Setting: Biochemistry and Nutrition Research Center, Faculty of Medicine, Universidad Nacional Mayor de San Marcos, Lima, Peru. Materials: Disodic p-nitrophenyl phosphate salt, glacial acetic acid, glycerol, tricloroacetic acid, sulfuric acid, ammonium molibdate, ascorbic acid, ammonium sulphate, sephadex G 75 (45-120), sulpho ethyl sephadex C-50 and ethylene diaminotetraacetic (EDTA) chemical reactives. Methods: Both Km and Vmax kinetic parameters were determined with p-nitrophenyl phosphate as substrate in presence of different concentrations of glycerol. The rate of formation of products was determined as a function of the concentration of such nucleophile. Main outcome measures: Glycerol effect on p-nitrophenyl phosphate hydrolysis. Results: Glycerol linearly increased pnitrophenol release at concentrations between 1,16 and 3,49M. Instead, inorganic phosphate formation, the second product, was not modified. Also, Km and Vmax values increased linearly between 0,58 and 2,32 M depending on glycerol concentrations. Conclusions: Analysis of modifications induced by glycerol on Km and Vmax values as well as on liberation velocity of the reaction products suggests a model in which low molecular weight acid phosphatase isolated from alpaca liver catalyses phosphomonoesters hydrolysis through an uni biordered mechanism, with formation of an enzyme phosphate complex that will be splitted by water or a nucleophile such a glycerol; in this model, k2 corresponds to a much higher value than k3 or k4 N.
Descritores: Catálise
Cinética
Fosfatase Ácida
Glicerol
-Epidemiologia Experimental
Responsável: PE1.1 - Oficina Universitária de Biblioteca


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Id: biblio-1022030
Autor: Fan, Shuanghu; Li, Kang; Yan, Yanchun; Wang, Junhuan; Wang, Jiayi; Qiao, Cheng; Yang, Ting; Jia, Yang; Zhao, Baisuo.
Título: A novel chlorpyrifos hydrolase CPD from Paracoccus sp. TRP: molecular cloning, characterization and catalytic mechanism
Fonte: Electron. j. biotechnol;31:10-16, Jan. 2018. graf, tab, ilust.
Idioma: en.
Projeto: National Natural Science Foundation of China; . Basic Research Fund of CAAS.
Resumo: Background: Biodegradation is a reliable approach for efficiently eliminating persistent pollutants such as chlorpyrifos. Despite many bacteria or fungi isolated from contaminated environment and capable of degrading chlorpyrifos, limited enzymes responsible for its degradation have been identified, let alone the catalytic mechanism of the enzymes. Results: In present study, the gene cpd encoding a chlorpyrifos hydrolase was cloned by analysis of genomic sequence of Paracoccus sp. TRP. Phylogenetic analysis and BLAST indicated that CPD was a novel member of organophosphate hydrolases. The purified CPD enzyme, with conserved catalytic triad (Ser155-Asp251-His281) and motif Gly-Asp-Ser-Ala-Gly, was significantly inhibited by PMSF, a serine modifier. Molecular docking between CPD and chlorpyrifos showed that Ser155 was adjacent to chlorpyrifos, which indicated that Ser155 may be the active amino acid involved in chlorpyrifos degradation. This speculation was confirmed by site-directed mutagenesis of Ser155Ala accounting for the decreased activity of CPD towards chlorpyrifos. According to the key role of Ser155 in chlorpyrifos degradation and molecular docking conformation, the nucleophilic catalytic mechanism for chlorpyrifos degradation by CPD was proposed. Conclusion: The novel enzyme CPD was capable of hydrolyze chlorpyrifos and Ser155 played key role during degradation of chlorpyrifos.
Descritores: Paracoccus/enzimologia
Clorpirifos/metabolismo
Esterases/metabolismo
-Organofosfatos/metabolismo
Biodegradação Ambiental
Catálise
Mutagênese
Clonagem Molecular
Análise de Sequência
Esterases/isolamento & purificação
Esterases/genética
Hidrólise
Metais/metabolismo
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1015957
Autor: Li, Jiajia; Xiao, Qiong; Huang, Yufeng; Ni, Hui; Wu, Changzheng; Xiao, Anfeng.
Título: Tannase application in secondary enzymatic processing of inferior Tieguanyin oolong tea
Fonte: Electron. j. biotechnol;28:87-94, July. 2017. tab, graf.
Idioma: en.
Projeto: National Natural Science Foundation of China; . Science and Technology Planning Project of Fujian Province.
Resumo: Background: Inferior Tieguanyin oolong tea leaves were treated with tannase. The content and bioactivity of catechins in extracts from the treated tea leaves were investigated to assess the improvement in the quality of inferior Tieguanyin oolong tea. Results: Analysis showed that after treatment, the esterified catechin content decreased by 23.5%, whereas non-galloylated catechin and gallic acid contents increased by 15.3% and 182%, respectively. The extracts from tannase-treated tea leaves showed reduced ability to bind to BSA and decreased tea cream levels. The extracts also exhibited increased antioxidant ability to scavenge OH and DPPH radicals, increased ferric reducing power, and decreased inhibitory effects on pancreatic α-amylase and lipase activities. Conclusions: These results suggested that tannase treatment could improve the quality of inferior Tieguanyin oolong tea leaves.
Descritores: Chá/enzimologia
Hidrolases de Éster Carboxílico/metabolismo
-Chá/metabolismo
Chá/química
Temperatura
Catálise
Catequina/análise
Folhas de Planta/enzimologia
Fermentação
Hidrólise
Lipase/antagonistas & inibidores
Lipase/metabolismo
Antioxidantes
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1015723
Autor: Wang, Jiayi; Lu, Lei; Feng, Fujuan.
Título: Combined strategies for improving production of a thermo-alkali stable laccase in Pichia pastoris
Fonte: Electron. j. biotechnol;28:7-13, July. 2017. tab, graf, ilus.
Idioma: en.
Projeto: National Natural Science Foundation of China; . Fundamental Research Funds for the Central Universities.
Resumo: Background: Laccases are copper-containing enzymes which have been used as green biocatalysts for many industrial processes. Although bacterial laccases have high stabilities which facilitate their application under harsh conditions, their activities and production yields are usually very low. In this work, we attempt to use a combinatorial strategy, including site-directed mutagenesis, codon and cultivation optimization, for improving the productivity of a thermo-alkali stable bacterial laccase in Pichia pastoris. Results: A D500G mutant of Bacillus licheniformis LS04 laccase, which was constructed by site-directed mutagenesis, demonstrated 2.1-fold higher activity when expressed in P. pastoris. The D500G variant retained similar catalytic characteristics to the wild-type laccase, and could efficiently decolorize synthetic dyes at alkaline conditions. Various cultivation factors such as medium components, pH and temperature were investigated for their effects on laccase expression. After cultivation optimization, a laccase activity of 347 ± 7 U/L was finally achieved for D500G after 3 d of induction, which was about 9.3 times higher than that of wild-type enzyme. The protein yield under the optimized conditions was about 59 mg/L for D500G. Conclusions: The productivity of the thermo-alkali stable laccase from B. licheniformis expressed in P. pastoris was significantly improved through the combination of site-directed mutagenesis and optimization of the cultivation process. The mutant enzyme retains good stability under high temperature and alkaline conditions, and is a good candidate for industrial application in dye decolorization.
Descritores: Pichia/metabolismo
Lacase/biossíntese
Lacase/genética
Bacillus licheniformis/enzimologia
-Temperatura
Leveduras
Estabilidade Enzimática
Catálise
Mutagênese
Lacase/metabolismo
Corantes/metabolismo
Concentração de Íons de Hidrogênio
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1008291
Autor: Xiao, Anfeng; Xiao, Qiong; Lin, Yan; Ni, Hui; Zhu, Yanbing; Cai, Huinong.
Título: Efficient immobilization of agarase using carboxyl-functionalized magnetic nanoparticles as support
Fonte: Electron. j. biotechnol;25:13-20, ene. 2017. ilus, graf.
Idioma: en.
Projeto: University-Enterprise Cooperation of Fujian Province University; . Major Science and Technology Programs and Special Topics of Fujian Province.
Resumo: Background: A simple and efficient strategy for agarase immobilization was developed with carboxyl-functionalized magnetic nanoparticles (CMNPs) as support. The CMNPs and immobilized agarase (agarase-CMNPs) were characterized by transmission electron microscopy, dynamic light scattering, vibrating sample magnetometry, scanning electron microscopy, X-ray diffraction, thermogravimetric analysis, and zeta-potential analysis. The hydrolyzed products were separated and detected by ESI-TOF-MS. Results: The agarase-CMNPs exhibited a regular spherical shape with a mean diameter of 12 nm, whereas their average size in the aqueous solution was 43.7 nm as measured by dynamic light scattering. These results indicated that agarase-CMNPs had water swelling properties. Saturation magnetizations were 44 and 29 emu/g for the carriers and agarase-CMNPs, respectively. Thus, the particles had superparamagnetic characteristics, and agarase was successfully immobilized onto the supports. Agaro-oligosaccharides were prepared with agar as substrate using agarase-CMNPs as biocatalyst. The catalytic activity of agarase-CMNPs was unchanged after six reuses. The ESI-TOF mass spectrogram showed that the major products hydrolyzed by agarase-CMNPs after six recycle uses were neoagarotetraose, neoagarohexaose, and neoagarooctaose. Meanwhile, the end-products after 90 min of enzymatic treatment by agarase-CMNPs were neoagarobiose and neoagarotetraose. Conclusions: The enhanced agarase properties upon immobilization suggested that CMNPs can be effective carriers for agarase immobilization. Agarase-CMNPs can be remarkably used in developing systems for repeated batch production of agar-derived oligosaccharides.
Descritores: Oligossacarídeos/metabolismo
Enzimas Imobilizadas
Nanopartículas de Magnetita/química
Glicosídeo Hidrolases/metabolismo
-Termogravimetria
Difração de Raios X
Estabilidade Enzimática
Catálise
Microscopia Eletrônica de Transmissão
Magnetometria
Difusão Dinâmica da Luz
Glicosídeo Hidrolases/química
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-837095
Autor: Wouters, Ana Dionéia.
Título: Carboidratos como matéria-prima para a preparação de substratos quirais: aplicações em catálise enantiosseletiva e processos diastereosseletivos / Carbohydrates as starting materials for the preparation of chiral substrates: applications in enantioselective and diastereoselective processes.
Fonte: São Paulo; s.n; 2013. 161 p. tab, graf, ilus.
Idioma: pt.
Tese: Apresentada a Universidade de São Paulo. Faculdade de Ciências Farmacêuticas para obtenção do grau de Doutor.
Resumo: O presente trabalho descreve o uso de carboidratos como materiais de partida para a preparação de catalisadores quirais e também de substratos quirais. Primeiramente estudos envolvendo a aplicação de amino álcoois derivados de carboidratos na arilação assimétrica de aldeídos, usando ácidos arilborônicos como fontes de grupos arila transferíveis, revelaram que um ligante preparado a partir da D-xilose mostrou-se bastante eficiente e conduziu aos produtos em excelentes rendimentos e altos excessos enantioméricos. Posteriormente a arilação de aldeídos derivados de carboidratos é descrita. Em alguns casos diastereosseletividades maiores que 20:1 foram observadas e a metodologia foi aplicada a síntese total da 7-epi-goniofufurona e análogos

The work described herein is centered on the use of carbohydrates as starting materials for the synthesis of chiral ligands and chiral sugar-derivatives. Initially, chiral amino alcohols were studied as ligands for the asymmetric arylation of aldehydes using aryl boronic acids as the source of transferable aryl groups. We found that a chiral ligand derived from D-xylose was very efficient and the desired products were obtained in excellent yields and enantiomeric excesses. In addition, the arylation of sugar-based aldehydes was also studied. In many cases, excellent diastereoselectivities of >20:1 were achieved and the methodology was employed in the total synthesis of 7-epi-goniofufurone and analogues
Descritores: Carboidratos/efeitos adversos
Substratos para Tratamento Biológico/efeitos adversos
-Aldeídos
Catálise
Química Farmacêutica
Síntese de Produtos
Responsável: BR40.1 - DBD - Divisão de Biblioteca e Documentacão do Conjunto das Químicas
BR40.1; T 615.19, W938c. 30100020213


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Id: lil-776701
Autor: Mielke, Grégore Iven; Malta, Deborah Carvalho; Sá, Gisele Balbino Araújo Rodrigues de; Reis, Rodrigo Siqueira; Hallal, Pedro Curi.
Título: Diferenças regionais e fatores associados à prática de atividade física no lazer no Brasil: resultados da Pesquisa Nacional de Saúde-2013 / Regional differences and correlates of leisure time physical activity in Brazil: results from the Brazilian National Health Survey-2013
Fonte: Rev. bras. epidemiol;18(supl.2):158-169, Out.-Dez. 2015. tab, graf.
Idioma: en.
Resumo: RESUMO: Objetivo: Analisar as diferenças regionais e os fatores associados à prática de atividade física no lazer em adultos participantes da Pesquisa Nacional de Saúde, de 2013. Métodos: Este estudo foi realizado com os dados da Pesquisa Nacional de Saúde, realizada em 2013 com uma amostra aproximada de 63.000 adultos (18+ anos). Para cada uma das cinco regiões do Brasil foi calculada a prevalência de adultos ativos no lazer, sendo classificados como ativos aqueles participantes que praticaram pelo menos 150 minutos por semana de atividades físicas no lazer. Resultados: A prevalência de ativos no lazer variou de 21,9% no Sul a 24,4% no Centro-Oeste. Homens foram 1,48 (IC95% 1,40 - 1,57) vezes mais ativos que as mulheres, sendo a região Norte aquela que apresentou maior diferença entre sexos. A prevalência de ativos foi 67% menor entre aqueles com 75+ anos quando comparado ao grupo de 18-24 anos, sendo que esta diferença foi mais acentuada na região Norte. Aqueles com maior grau de instrução foram, em média, três vezes mais ativos que os participantes com menor grau de instrução. Em termos de grau de instrução, a menor diferença observada ocorreu no Nordeste. Conclusões: Apesar das pequenas variações na prevalência de prática de atividade física no lazer entre as regiões, quando são considerados subgrupos populacionais, diferenças importantes são observadas. Estes resultados sugerem a necessidade de ações de promoção de atividade física com diferentes abordagens em cada uma das cinco regiões do Brasil.

ABSTRACT: Objective: To analyze the regional differences and factors associated with physical activity during the leisure time in the adult participants of the National Health Survey, 2013. Methods: This study was carried out with the data from the National Health Survey, conducted in 2013 with an approximate sample of 63,000 adults (18+ years). For each of the five regions of Brazil, the prevalence of physically active adults during the leisure time was calculated, and the participants were classified as active if they practiced at least 150 minutes per week of physical activity during leisure time. Results: The prevalence of individuals who were active during the leisure time varied from 21.9% in the south to 24.4% in the midwest. The men were 1.48 (95%CI 1.40-1.57) times more active than women, with the northern region showing the highest difference between the sexes. The prevalence of active individuals was 67% lower among those aged 75+ years when compared with the 18-24 age group, and this difference was more marked in the north. Those with higher levels of education were on average three times more active than the participants with lower education levels. In terms of education level, the lowest difference was observed in the northeast. Conclusion: Despite the slight variations in the prevalence of physical activity during the leisure time among the regions, when population subgroups are considered, important differences were observed. These results suggest the need for promotion initiatives on physical activity with different approaches in each of the five regions of Brazil.
Descritores: Materiais Biocompatíveis
Hidrogéis
Temperatura
-Catálise
Cinética
Tipo de Publ: Research Support, N.I.H., Extramural
Responsável: BR1.1 - BIREME



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde