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Pesquisa : D08.811.277.450.420.200 [Categoria DeCS]
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Id: biblio-1045993
Autor: Zeeshan, Nadia; Naz, Saher; Naz, Shumaila; Afroz, Amber; Zahur, Muzna; Zia, Safia.
Título: Heterologous expression and enhanced production of ß-1, 4-glucanase of Bacillus halodurans C-125 in Escherichia coli
Fonte: Electron. j. biotechnol;34:29-36, july. 2018. ilus, tab, graf.
Idioma: en.
Projeto: Higher Education Commission, Pakistan (HEC).
Resumo: Background: Recombinant DNA technology enables us to produce proteins with desired properties and insubstantial amount for industrial applications. Endo-1, 4-ß-glucanases (Egl) is one of the major enzyme involved in degradation of cellulose, an important component of plant cell wall. The present study was aimed at enhancing the production of endo-1, 4-ß-glucanases (Egl) of Bacillus halodurans in Escherichia coli. Results: A putative Egl gene of Bacillus Halodurans was expressed in E. coli by cloning in pET 22b (+). On induction with isopropyl-b-D-1-thiogalactopyranoside, the enzyme expression reached upto ~20% of the cell protein producing 29.2 mg/liter culture. An increase in cell density to 12 in auto-inducing LB medium (absorbance at 600 nm) enhanced ß-glucanase production up to 5.4 fold. The molecular mass of the enzyme was determined to be 39 KDa, which is nearly the same as the calculated value. Protein sequence was analyzed by CDD, Pfam, I TASSER, COACH, PROCHECK Servers and putative amino acids involved in the formation of catalytic, substrate and metal binding domains were identified. Phylogenetic analysis of the ß-glucanases of B. halodurans was performed and position of Egl among other members of the genus Bacillus producing endo-glucanases was determined. Temperature and pH optima of the enzyme were found to be 60°C and 8.0, respectively, under the assay conditions. Conclusion: Production of endo-1, 4 ß-glucanase enzymes from B. halodurans increased several folds when cloned in pET vector and expressed in E. coli. To our knowledge, this is the first report of high-level expression and characterization of an endo-1, 4 ß-glucanases from B. halodurans.
Descritores: Bacillus/enzimologia
Celulases/biossíntese
-Temperatura
Estabilidade Enzimática
Expressão Gênica
Parede Celular/enzimologia
Reação em Cadeia da Polimerase
Clonagem Molecular
Celulases/isolamento & purificação
Celulases/metabolismo
Escherichia coli/metabolismo
Células Vegetais/enzimologia
Concentração de Íons de Hidrogênio
Hidrólise
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1290558
Autor: Mata, Gerardo; Salmones, Dulce; Pérez-Merlo, Rosalía.
Título: Actividad de las enzimas hidrolíticas en cepas del hongo shiitake (Lentinula edodes) cultivadas en pulpa de café / Hydrolytic enzyme activities in shiitake mushroom (Lentinula edodes) strains cultivated on coffee pulp
Fonte: Rev. argent. microbiol;48(3):191-195, set. 2016. graf.
Idioma: en.
Resumo: Se estudió la producción de enzimas hidrolíticas (celulasas, laminarinasas y xilanasas) en cultivos de Lentinula edodes en pulpa de café estéril. Se tomaron muestras de sustrato colonizado por el micelio después de 7, 14, 21, 28 y 35 días de incubación a 25°C (W1 a W5) y durante el período de fructificación en diferentes etapas: formación de primordios (PF), primera cosecha (H) y una semana después de la primera cosecha (PH). La actividad enzimática fue menor al inicio del crecimiento micelial y mostró mayores niveles en la formación y el desarrollo de basidiomas. Durante la etapa reproductiva del hongo, las muestras se sometieron a un tratamiento de remojo. Sin embargo, no fue posible relacionar este tratamiento con el aumento de la producción de enzimas. Los niveles de actividad enzimática sugieren que la secreción de las enzimas estudiadas no influye en la capacidad de adaptación de las cepas al sustrato

Hydrolytic enzyme production (cellulases, laminarinases and xylanases) was studied in cultures of Lentinula edodes on sterilized coffee pulp. Samples of substrate colonized by mycelia were taken after 7, 14, 21, 28 and 35 days of incubation at 25°C (W1 to W5) and during the fruiting period at different stages: formation of primordia (PF), first harvest (H) and one week after the first harvest (PH). The enzymatic activity was lower during the early mycelial growth and showed higher levels during the formation and development of fruiting bodies. During the reproductive stage of the fungus, the samples were subjected to a soaking treatment; however, it was not possible to relate this soaking treatment to the increase in enzyme production. The levels of enzymatic activity suggest that secretion of the studied enzymes does not influence the adaptability of the strains to the substrate
Descritores: Cogumelos Shiitake/crescimento & desenvolvimento
Cogumelos Shiitake/enzimologia
Enzimas/análise
-Celulases/isolamento & purificação
Tipo de Publ: Estudo de Avaliação
Estudo Observacional
Responsável: AR635.1 - FCVyS - Servicio de Información y Documentación


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Id: biblio-1132254
Autor: Salazar, Ludmila Noskoski; Astolfi, Viviane; Ogimbosvski, Tailan Antonio; Daronch, Naionara Ariete; Zeni, Jamile; Junges, Alexander; Cansian, Rogério Luis; Backes, Geciane Toniazzo.
Título: Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
Fonte: Braz. arch. biol. technol;63:e20170710, 2020. tab, graf.
Idioma: en.
Resumo: Abstract (1) Background: The aim of this study was to evaluate the production and partial characterization of xylanase and avicelase by a newly isolated Penicillium sp. in solid-state fermentation, using soybean hulls as substrate. (2) Methods: Temperature, time, number of spores, and substrate moisture on xylanase and avicelase bioproduction were evaluated, maximizing activity with 30°C, 1x106 spores/g substrate, 14 and 7 days of fermentation with 70 and 76% substrate moisture contents, for xylanase and avicelase, respectively. (3) Results: Different solvents, temperatures, and agitation in the enzymatic extraction were evaluated, obtaining higher activities, 430.77 and 26.77 U/g for xylanase and avicelase using 30 min extraction and 0.05 M citrate buffer solution (pH 4.5 ), respectively at 60°C and 175 rpm and 50°C and 125 rpm. The optimum pH and temperature for enzymatic activity determination were 5.3 and 50°C. Enzyme extract stability was evaluated, obtaining higher stability with pH between 4.5 and 5.5, higher temperature of up to 40°C. The kinetic thermal denaturation (Kd), half-life time, D-value, and Z-value were similar for both enzymes. The xylanase Ed value (89.1 kJ/mol) was slightly lower than the avicelase one (96.7 kJ/mol), indicating higher thermostability for avicelase. (4) Conclusion: In this way, the production of cellulases using alternative substrates is a way to reduce production costs, since they represent about 10% of the world demand of enzymes, with application in animal feed processing, food production and breweries, textile processing, detergent and laundry production, pulp manufacturing and the production of biofuels.
Descritores: Penicillium/isolamento & purificação
Penicillium/enzimologia
Soja/microbiologia
Xilosidases/biossíntese
Celulases/biossíntese
-Temperatura
Fatores de Tempo
Substratos para Tratamento Biológico
Responsável: BR1.1 - BIREME


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Id: biblio-1146988
Autor: Marim, Renan Alberto; Avelino, Katielle Vieira; Halabura, Marisangela Isabel Wietzikoski; Araújo, Nelma Lopes; Santana, Thiago Teodoro; Linde, Giani Andrea; Colauto, Nelson Barros; Valle, Juliana Silveira do.
Título: Lentinus crinitus response to blue light on carbohydrate-active enzymes / Resposta de Lentinus crinitus à luz azul em enzimas ativas por carboidratos
Fonte: Biosci. j. (Online);36(3):924-931, 01-05-2020. tab.
Idioma: en.
Resumo: Fungi are capable of sensing light from ultraviolet to far-red and they use light as a source of information about the environment anticipating stress and adverse conditions. Lentinus crinitus is a lignin-degrading fungus which produces laccase and other enzymes of biotechnological interest. The effect of blue light on fungal enzymatic activity has been studied; however, it has not been found studies on the effect of the blue light on carbohydrate-active enzymes and on mycelial biomass production of L. crinitus. We aimed to investigate carbohydrate-active enzymes activity and mycelial biomass production of L. crinitus cultivated under continuous illumination with blue light. L. crinitus was cultivated in malt extract medium in the dark, without agitation, and under continuous illumination with blue light-emitting diodes. The blue light reduced the total cellulase, pectinase and xylanase activities but increased the endoglucanase activity. Blue light reduced the mycelial growth of L. crinitus in 26% and the enzymatic activity-to-mycelial biomass ratio (U mg-1 dry basis) increased in 10% total cellulase, 33% endoglucanase, and 16% pectinase activities. Also, it is suggested that L. crinitus has a photosensory system and it could lead to new process of obtaining enzymes of biotechnological interest.

Fungos são capazes de sentir a luz com comprimentos de onda que variam do ultravioleta ao infravermelho e usam a luz como fonte de informação sobre o ambiente, antecipando condições adversas e de estresse. Lentinus crinitus é um fungo ligninolítico que produz lacase e outras enzimas de interesse biotecnológico. O efeito da luz azul na atividade enzimática de fungos já foi estudado, contudo, ainda não há estudos sobre o efeito da luz azul na produção de enzimas ativas sobre carboidratos (CAZymes, carbohydrate-active enzymes) e de biomassa micelial de L. crinitus. O objetivo deste estudo foi investigar a avitivade de CAZymes e a produção de biomassa micelial de L. crinitus cultivado sob iluminação continua com luz azul. L. crinitus foi cultivado em meio extrato de malte, sem agitação, na ausência de luz e sob luz continua fornecida por diodos emissores de luz azul. A luz azul reduziu a atividade de cellulase total, pectinase e xilanase, mas aumentou a atividade de endoglucanase. A luz azul reduziu o crescimento micelial de L. crinitus em 26% e aumentou a razão atividade enzimática/biomassa micelial (U mg-1 em base seca) de cellulase total em 10%, endoglucanase em 33% e pectinase em 16%. Além disso, sugere-se que L. crinitus possua um sistema fotossensorial que poderia ser explorado para a otimização de bioprocessos que visam a obtenção de enzimas de interesse biotecnológico.
Descritores: Poligalacturonase
Lentinula
Celulases
Luz
Responsável: BR396.1 - Biblioteca Central


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Id: biblio-1129781
Autor: Vaz, D. P; Dalólio, F. S; Moreira, J; Pinheiro, S. R. F; Lara, L. J. C; Valadares, L. R; Cruz, P. J. R.
Título: Características do trato digestivo, metabolizabilidade e retenção de nutrientes em frangos de corte alimentados com complexo enzimático / Characteristics of the digestive tract, metabolizability and nutrient retention in broilers fed enzymatic complex
Fonte: Arq. bras. med. vet. zootec. (Online);72(3):1069-1074, May-June, 2020. tab.
Idioma: pt.
Resumo: The objective was to evaluate the digestive tract characteristics, metabolizability and nutrient retention of broilers fed diets supplemented with enzyme complex (EC). To evaluate the characteristics of the digestive tract 600 female Cobb 500 birds were used, distributed in a completely randomized design, with 5 inclusion levels of the EC (0; 100, 200, 300 and 400 g/ton) and 6 replicates of 20 birds each. To evaluate the metabolizability and the retention of nutrients 200 female Cobb 500 birds at 15 days of age were used, distributed in a completely randomized design with 5 levels of supplementation of the EC and 4 replicates of 10 birds each. No significant effects (P>0.05) were observed for the supplementation of the EC in the intestinal pH, digestive organ weight, intestinal length and metabolizable coefficients of dry matter and crude protein. The metabolizable coefficient of ethereal extract was influenced in a quadratic decreasing form (P<0.01). The metabolizable coefficients of calcium (Ca) and phosphorus (P) were influenced in a quadratic increase (P<0.01), resulting in increased Ca retention in 21.39% and P in 9.56%. Supplementation of the EC in broiler diets improves the metabolizability and retention of P and Ca, without affecting the other parameters evaluated.(AU)
Descritores: Nutrientes/administração & dosagem
Galinhas/metabolismo
Trato Gastrointestinal/metabolismo
Enzimas/administração & dosagem
-Peptídeo Hidrolases
Suplementos Nutricionais/análise
Celulases
Limites: Animais
Responsável: BR68.1 - Biblioteca Virginie Buff D'Ápice


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Id: biblio-1087169
Autor: Rodríguez-Mendoza, Johan; Santiago-Hernández, Alejandro; Alvarez-Zúñiga, María Teresa; Gutiérrez-Antón, Marina; Aguilar-Osorio, Guillermo; Hidalgo-Lara, María Eugenia.
Título: Purification and biochemical characterization of a novel thermophilic exo-ß-1, 3-glucanase from the thermophile biomass-degrading fungus Thielavia terrestris Co3Bag1
Fonte: Electron. j. biotechnol;41:60-71, sept. 2019. graf, tab, ilus.
Idioma: en.
Projeto: Departamento de Biotecnología y Bioingeniería, CINVESTAV-IPN, México.
Resumo: Background: The aim of this work was to purify and characterize exo-ß-1,3-glucanase, namely, TtBgnA, from the thermophilic fungus Thielavia terrestris Co3Bag1 and to identify the purified enzyme. Results: The thermophilic biomass-degrading fungus T. terrestris Co3Bag1 displayed ß-1,3-glucanase activity when grown on 1% glucose. An exo-ß-1,3-glucanase, with an estimated molecular mass of 129 kDa, named TtBgnA, was purified from culture filtrates from T. terrestris Co3Bag1. The enzyme exhibited optimum activity at pH 6.0 and 70°C and half-lives (t1/2) of 54 and 37 min at 50 and 60°C, respectively. Substrate specificity analysis showed that laminarin was the best substrate studied for TtBgnA. When laminarin was used as the substrate, the apparent KM and Vmax values were determined to be 2.2 mg mL-1 and 10.8 U/mg, respectively. Analysis of hydrolysis products by thin-layer chromatography (TLC) revealed that TtBgnA displays an exo mode of action. Additionally, the enzyme was partially sequenced by tandem mass spectrometry (MS/MS), and the results suggested that TtBgnA from T. terrestris Co3Bag1 could be classified as a member of the GH-31 family. Conclusions: This report thus describes the purification and characterization of TtBgnA, a novel exo-ß-1,3-glucanase of the GH-31 family from the thermophilic fungus T. terrestris Co3Bag1. Based on the biochemical properties displayed by TtBgnA, the enzyme could be considered as a candidate for potential biotechnological applications.
Descritores: Sordariales/enzimologia
Glucana 1,3-beta-Glucosidase/química
-Temperatura
Estabilidade Enzimática
Celulases
Glucana 1,3-beta-Glucosidase/isolamento & purificação
Eletroforese em Gel de Poliacrilamida
Espectrometria de Massas em Tandem
Ensaios Enzimáticos
Concentração de Íons de Hidrogênio
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1053552
Autor: Smuga-Kogut, Malgorzata; Piskier, Tomasz; Walendzik, Bartosz; Szymanowska-Powalowska, Daria.
Título: Assessment of wasteland derived biomass for bioethanol production
Fonte: Electron. j. biotechnol;41:1-8, sept. 2019. tab, ilus, graf.
Idioma: en.
Projeto: National Science Centre as part of MINIATURA 1.
Resumo: Background: The bioethanol produced from biomass is a promising alternative fuel. The lignocellulose from marginal areas or wasteland could be a promising raw material for bioethanol production because it is present in large quantities, is cheap, renewable and has favorable environmental properties. Despite these advantages, lignocellulosic biomass is much more difficult to process than cereal grains, due to the need for intensive pretreatment and relatively large amounts of cellulases for efficient hydrolysis. Therefore, there is a need to develop an efficient and cost-effective method for the degradation and fermentation of lignocellulosic biomass to ethanol. Results: The usefulness of lignocellulosic biomass from wasteland for the production of bioethanol using pretreatment with the aid of ionic liquids of 1-ethyl-3-methylimidazolium acetate and 1-ethyl-3-methylimidazolium chloride was evaluated in this study. The pretreatment process, enzymatic hydrolysis and alcoholic fermentation lasted a total of 10 d. The largest amounts of bioethanol were obtained from biomass originating from agricultural wasteland, in which the dominant plant was fireweed (Chamaenerion angustifolium) and from the field where the common broom (Cytisus scoparius) was the dominant. Conclusions: The plants such as fireweed, common broom, hay and goldenrod may be useful for the production of liquid biofuels and it would be necessary in the further stage of research to establish and optimize the conditions for the technology of ethyl alcohol producing from these plant species. Enzymatic hydrolysis of biomass from agricultural wastelands results in a large increase in fermentable sugars, comparable to the enzymatic hydrolysis of rye, wheat, rice or maize straw.
Descritores: Solo/química
Biomassa
Etanol/metabolismo
-Biodegradação Ambiental
Celulases/análise
Enzimas/metabolismo
Líquidos Iônicos
Biocombustíveis
Hidrólise
Lignina/análise
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1049943
Autor: Pena Júnior, Carlos Eduardo.
Título: Efeito das glicosilações sobre a estrutura e dinâmica da celulase Cel7A de Trichoderma reesei / Effect of glycosylations on the structure and dynamics of Cel7A cellulase from Trichoderma reesei.
Fonte: Rio de Janeiro; s.n; 2019. xiv, 152 p. ilus.
Idioma: pt.
Tese: Apresentada a Instituto Oswaldo Cruz para obtenção do grau de Doutor.
Resumo: Celulases fúngicas têm sido usadas para degradar a biomassa lignocelulósica para a produção de bioetanol. Celulases industriais como Cel7A de Trichoderma reesei (TrCel7A) são críticas neste processo. A compreensão da estrutura e dinâmica é crucial para a reengenharia da atividade celulolítica. Esta enzima é formada por dois domínios ligados por um linker flexível e altamente glicosilado. No entanto, a flexibilidade do linker tem dificultado a determinação da estrutura completa da Cel7A. Assim, na ausência de dados experimentais de alta resolução, aplicamos a modelagem integrativa para construir um modelo da enzima completa. Em seguida, estudamos os efeitos da glicosilação na estrutura e dinâmica da apo TrCel7A por meio de simulações. A análise da dinâmica essencial mostrou que a O-glicosilação no linker levou à estabilização da dinâmica global da proteína. Os glicanos O-ligados parecem restringir a distribuição dos ângulos diedros desta região, selecionando conformações mais alongadas. Além da flexibilidade reduzida, os movimentos interdomínios funcionais foram preservados no sistema glicosilado. Em contraste, observamos grande plasticidade conformacional na ausência de glicosilação, mas os domínios funcionais frequentemente colapsaram. Nós relatamos aqui evidências de que a flexibilidade dirigida no linker de Cel7A por mutações pontuais, incluindo modificações de sítios de glicosilação, poderia ser uma estratégia promissora para melhorar a atividade da celulase. (AU)
Descritores: Trichoderma
Glicosilação
Mutagênese Insercional
Celulases
Limites: Humanos
Responsável: BR15.1 - Biblioteca de Ciências Biomédicas


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Id: biblio-1039268
Autor: Cardoso, Wilton Soares; Queiroz, Paula Viana; Tavares, Gabriella Peterlini; Santos, Fernando Almeida; Soares, Filippe Elias de Freitas; Kasuya, Maria Catarina Megumi; Queiroz, José Humberto de.
Título: Multi-enzyme complex of white rot fungi in saccharification of lignocellulosic material
Fonte: Braz. j. microbiol;49(4):879-884, Oct.-Dec. 2018. tab, graf.
Idioma: en.
Resumo: ABSTRACT The multi-enzyme complex (crude extract) of white rot fungi Pleurotus ostreatus, Pleurotus eryngii, Trametes versicolor, Pycnosporus sanguineus and Phanerochaete chrysosporium were characterized, evaluated in the hydrolysis of pretreated pulps of sorghum straw and compared efficiency with commercial enzyme. Most fungi complexes had better hydrolysis rates compared with purified commercial enzyme.
Descritores: Proteínas Fúngicas/química
Sorghum/química
Celulases/química
Fungos/enzimologia
Lignina/química
-Proteínas Fúngicas/metabolismo
Caules de Planta/microbiologia
Caules de Planta/química
Sorghum/microbiologia
Celulases/metabolismo
Biocatálise
Fungos/química
Hidrólise
Lignina/metabolismo
Responsável: BR1.1 - BIREME


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Martins, Meire Lelis Leal
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Id: biblio-849049
Autor: Oliveira, Luciana Ribeiro Coutinho; Barbosa, João Batista; Martins, Meire Lelis Leal; Martins, Marco Antônio.
Título: Extracellular production of avicelase by the thermophilic soil bacterium Bacillus sp SMIA-2 / Produção de avicelase extracelular pela bactéria termofílica Bacillus sp SMIA-2
Fonte: Acta sci., Biol. sci;36(2):215-222, abr.- jun. 2014. ilus, tab.
Idioma: en.
Resumo: Nowadays, the isolation of new bacterial strains that produce enzymes with novel properties is a subject of great relevance to the scientific community. This study, in order to search for producers of new cellulase strains, investigated the avicelase production by thermophilic Bacillus sp. strain SMIA-2. The best avicelase activity was observed in a culture medium containing 0.5% (w v-1) avicel and 0.5% (w v-1) corn steep liquor with initial pH 7.5- 8.0 incubated at 50 oC. When avicel was replaced in the medium by the treated sugarcane bagasse (0.5%, w v-1) the avicelase activity levels were not affected. Studies on the avicelase characterization revealed that the optimum pH of the enzyme was found to be 8.5 and the enzyme retained more than 80% of its activity after incubation at room temperature for 2h at pH 6.5-8.5. The optimum temperature of this enzyme was 70oC and the enzyme retained 67% of the original activity after 20 min. of heat treatment at 70oC. Avicelase was stimulated by Mn2+ and Co2+, whereas Hg2+ greatly inhibited the enzyme activity.

Atualmente, o isolamento de estirpes de bactérias que produzem enzimas com novas propriedades é um tema de grande relevância para a comunidade científica. Este trabalho, buscando por novas cepas produtoras de celulases, investigou a produção de avicelases pelo termofílico Bacillus sp. cepa SMIA-2. A melhor atividade da enzima foi obtida em uma cultura contendo 0,5% (p v-1) avicel e 0,5% (p v-1) água de maceração de milho com pH inicial de pH 7,5-8,0 e incubada a 50oC. A substituição da avicel no meio de cultura pelo bagaço de cana- de- açúcar tratado (0,5%, p v-1) não afetou os níveis de atividade da avicelase. Estudos sobre a caracterização da avicelase revelaram que o pH para atividade ótima da enzima foi 8,5 e que a mesma reteve mais de 80% de sua atividade após ser incubada à temperatura ambiente por 2 h a pH 6,5-8,5. A temperatura ótima da avicelase foi 70oC e a enzima reteve 67% da sua atividade original após 20 min. de incubação a 70oC. A avicelase foi estimulada pelos íons Mn2+ e Co2+, ao passo que Hg2+ inibiu a atividade da enzima.
Descritores: Bacillus
Celulases
Saccharum
Zea mays
Responsável: BR513.1 - Biblioteca Central



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