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Pesquisa : G02.494 [Categoria DeCS]
Referências encontradas : 139 [refinar]
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Id: biblio-1021325
Autor: Al-Soqeer, Abdulrahman A; Alsubaie, Qasi D; Motawei, Mohamed I; Mousa, Hassan M; Abdel-Salam, Ahmed M.
Título: Isolation and identification of allergens and biogenic amines of Prosopis juliflora genotypes
Fonte: Electron. j. biotechnol;30:24-32, nov. 2017. tab, ilus, graf.
Idioma: en.
Resumo: Background: Prosopis, or mesquite (Prosopis juliflora (Sw.) DC.), was introduced in Saudi Arabia several decades ago and is heavily used in street, roadside, and park plantations. It shows great adaptation to the prevailing climatic conditions such as high temperature, severe drought, and salinity and spreads naturally in many parts of the Kingdom. This research was conducted to isolate allergen proteins and biogenic amines from the pollen grains of P. juliflora genotypes in Saudi Arabia from two regions, namely Al-Qassim and Eastern regions. Results: The results showed that 18 different allergen proteins were detected in P. juliflora genotypes, with molecular weight ranging from 14 to 97 kDa. Moreover, P. juliflora genotypes from the two studied regions contained eight biogenic amines, namely histamine, tyramine, tryptamine, ß-phenylethylamine, butricine, codapherine, spermidine, and spermine. All genotypes from the Al-Qassim region were found to contain all eight amines, while in the Eastern region, histamine was absent in three genotypes, spermine was absent in six genotypes, and spermidine was absent in three genotypes. Genotypes B23, E20, and E21 had the lowest biogenic amine quantity. Conclusions: All identified proteins from mesquite trees from both regions (Eastern and Al-Qassim) cause allergies in patients who are sensitive to pollen grains. Bioamines, except histamine and tyramine, were recorded at varying concentrations in different genotypes.
Descritores: Pólen/química
Aminas Biogênicas/isolamento & purificação
Alérgenos/isolamento & purificação
Prosopis
-Proteínas de Plantas/isolamento & purificação
Histamina/isolamento & purificação
Tiramina/isolamento & purificação
Cromatografia Líquida de Alta Pressão
Eletroforese em Gel de Poliacrilamida
Genótipo
Peso Molecular
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1016095
Autor: Fitriani, Dewi; Rohman, M Saifur; Prijambada, Irfan D.
Título: Proteolytic activity of recombinant DegP from Chromohalobacter salexigens BKL5
Fonte: Electron. j. biotechnol;29:7-12, sept. 2017. ilus, graf, tab.
Idioma: en.
Resumo: Background: DegP is a serine protease that specifically cleaves and refolds unfolding proteins in the periplasmic space of the cells. To date, there is no information regarding DegP from halophilic bacteria. Chromohalobacter salexigens BKL5 is a moderately halophilic bacterium that has the ability to grow in a media containing more than 15% salt. Therefore, the objectives of this work were to clone and overexpress DegP-encoding gene from C. salexigens BKL5 and characterize its biochemical properties. Results: DegP-encoding gene was overexpressed in Escherichia coli BL21(DE3) CodonPlus in an active form. SDS-PAGE analysis showed that the molecular weight of the recombinant DegP was 45 kDa. Size-exclusion chromatography analysis suggested that recombinant DegP was present in two multimeric states, hexameric and dodecameric, with molecular weights of 297.9 and 579.12 kDa, respectively. Both conformations were enzymatically active when casein was used as substrate for enzymatic assay. Circular dichroism analysis showed that recombinant DegP was composed of 0.21­0.29 helical content, which was comparable to the helical content in the crystal structure of E. coli DegP. The basic/acidic residue ratio of recombinant DegP was 0.56, which was slightly higher than that of DegP from extreme halophiles (average, 0.45) but significantly lower than that of DegP from nonhalophiles (average, 0.94). Conclusions: Recombinant DegP from C. salexigens BKL5 showed proteolytic activity when ß-casein was used as a substrate. In silico analysis indicated that recombinant DegP had characteristics similar to those of halophilic proteins depending on its amino acid composition.
Descritores: Serina Endopeptidases/genética
Proteínas Periplásmicas/genética
Chromohalobacter/enzimologia
Proteólise
Proteínas de Choque Térmico/genética
-Proteínas Recombinantes
Serina Endopeptidases/metabolismo
Caseínas
Cromatografia em Gel
Dicroísmo Circular
Clonagem Molecular
Proteínas Periplásmicas/metabolismo
Eletroforese em Gel de Poliacrilamida
Escherichia coli
Salinidade
Chromohalobacter/genética
Proteínas de Choque Térmico/metabolismo
Peso Molecular
Responsável: CL1.1 - Biblioteca Central


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Id: lil-719507
Autor: Antitupa, Isidro; Quispe, William; Mayo, Jhon; Valverde, Fanny; Sanchez, Elizabeth.
Título: Purificación de la fracción antigénica 27-28 KDa a partir del antígeno metabólico secretado-excretado de Fasciola hepatica / Purification of antigenic fraction 27-28 KDa from the metabolic antigen from metabolic secreted-excreted from Fasciola hepatica
Fonte: Rev. peru. med. exp. salud publica;31(2):288-291, abr.-jun. 2014. ilus.
Idioma: es.
Resumo: En el presente estudio, las fracciones antigénicas de 27-28 KDa de Fasciola hepatica fueron purificadas por cromatografía de exclusión molecular para su aplicación en el diagnóstico de la fascioliasis humana. Se obtuvieron antígenos de excreción y secreción a partir de fasciolas adultas vivas obtenida de hígado de ovino y bovino, y cultivados en medio mínimo esencial. La reactividad y eficacia del antígeno purificado fueron evaluadas por la prueba de inmunoblot empleando cuatro sueros con fascioliasis humana; cuatro sueros con otras parasitosis, y dos sueros negativos. Se concluye que las fracciones antigénicas purificadas no presentan reacción cruzada con otras parasitosis, por inmunoblot, por lo que se considera a las proteínas purificadas como potenciales candidatas a ser utilizadas para el diagnóstico de fascioliasis humana.

Antigenic fractions of 27-28 kDa from Fasciola hepatica were purified by size-exclusion chromatography for use in the diagnosis of human fasciolosis. Excretion and secretion antigens were obtained from living adult flukes collected from sheep and cattle liver, and cultured in minimum essential medium. The reactivity of the purified antigen and efficacy were assessed by immunoblot test using four sera with human fascioliasis; four sera with other parasites, and two negative sera. We conclude that the purified antigenic fractions do not cross-react with other parasites by immunoblot. Therefore, purified proteins are considered as potential candidates to be used for the diagnosis of human fascioliasis.
Descritores: Antígenos de Helmintos/isolamento & purificação
Fasciola hepatica/imunologia
-Antígenos de Helmintos/metabolismo
Fasciola hepatica/metabolismo
Fasciolíase/diagnóstico
Peso Molecular
Limites: Seres Humanos
Animais
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: biblio-994930
Autor: Vasquez Mejia, Sandra Milena; De Francisco, Alicia; Manique Barreto, Pedro Luiz; Mattioni, Bruna; Zibetti, André Wüst; Molognoni, Luciano; Daguer, Heitor.
Título: Physicochemical comparison of commercial VS. extracted ß-glucans and structural characterization after enzymatic purification / Comparación fisicoquímica entre ß-glucanos comerciales y extraídos, y caracterización estructural después de purificación enzimática
Fonte: Vitae (Medellín);25(1):26-36, 2018. Ilustraciones.
Idioma: en.
Resumo: Background: ß-glucans (1-3: 1-4) are soluble fibers applied to foods due to their technological properties (water binding capacity, viscosity, emulsification and stabilization) and their beneficial effects on health. The functional properties of ß-glucans can be lost during the extraction and purification processes. The high viscosity of ß-glucans is related to a high molecular weight and its physiological properties in the intestine. Therefore, to characterize the fiber after its extraction and purification is fundamental to understand its possible applications in foods. Objectives: characterize ß-glucans extracted (EßG) and compare them with three commercial ß-glucans (CßG-A, CßG-B and CßG-C) to identify its possible applications in foods and to evaluate if enzymatic purification affects molecular and structurally the ß-glucans. Methods: barley ß-glucans were extracted (EßG), characterized by chemical analyzes, rheological behavior, and color, and compared to three commercial ß-glucans samples. Then, the extract was purified and its structural and molecular characteristics were calculated. Results: EßG contained 64.38 ± 3.54% of ß-glucans, high starch contamination (12.70 ± 1.73%), high content of calcium (8894 mg/kg), pseudoplastic behavior, and dark color (L* = 52.77 ± 0.7). All commercial samples showed low starch contamination, lighter color, and Newtonian behavior. After purification starch and protein contamination decreased (0.85 ± 0.46% and 5.50 ± 0.12% respectively), increased the content of ßG (69.45 ± 0.81%) and increased brightness (L* = 92.60 ± 1.70). Purified ß-glucans (PßG) showed a molar weight of 690 ± 1.6 kDa and species with degree polymerization 3 (DP3) to 11 (DP11) were identified on the structure. Conclusions: EßG extracts before the purification presented a high viscosity and contamination. The enzymatic purification process was effective and allowed to maintain a high molar mass of PßG and its distinctive molecular structures (species with DP3 and DP4). The commercial samples CßG-A and CßG-B showed a low content of ß-glucans. Finally, CßG-C presented the best physicochemical and rheological properties for its subsequent application in food.

Antecedentes: los ß-glucanos (1-3: 1-4) son fibras solubles aplicadas a los alimentos debido a sus propiedades tecnológicas (capacidad de retención de agua, viscosidad, emulsificación y estabilización) y a sus efectos beneficiosos en la salud. Las propiedades funcionales de los ß-glucanos pueden perderse durante los procesos de extracción y purificación. La alta viscosidad de los ß-glucanos está relacionada con un alto peso molecular y con sus propiedades fisiológicas en el intestino. Por lo tanto, caracterizar la fibra después de su extracción y purificación es fundamental para comprender sus posibles aplicaciones en alimentos. Objetivos: caracterizar ß-glucanos extraídos (EßG) y compararlos con tres marcas comerciales (CßG-A, CßG-B y CßG-C) para identificar su futura aplicación en alimentos y evaluar si la purificación enzimática afecta molecular y estructuralmente los ß-glucanos. Métodos: se extrajeron ß-glucanos de cebada (EßG), caracterizados por análisis químicos, comportamiento reológico y color, y se compararon con tres muestras comerciales. Posteriormente, el extracto (EßG) se purificó y se identificaron sus características estructurales y su peso molecular. Resultados: EßG contenía 64.38 ± 3.54% de ß-glucanos, alta contaminación con almidón (12.70 ± 1.73%), alto contenido de calcio (8894 mg / kg), comportamiento pseudoplástico y color oscuro (L* = 52.77 ± 0.7). Todas las muestras comerciales mostraron una baja contaminación con almidón, color más claro y comportamiento newtoniano. Después de la purificación de EßG, la contaminación con almidón y proteína disminuyó (0.85 ± 0.46% y 5.50 ± 0.12%, respectivamente), aumentó el contenido de ßG (69.45 ± 0.81%) y aumentó su luminosidad (L* = 92.60 ± 1.70). Los ß-glucanos purificados (PßG) mostraron un peso molar de 690 ± 1,6 kDa y se identificaron en la estructura especies con grado de polimerización desde 3 (GP3) hasta 11 (GP11). Conclusiones: los EßG antes de la purificación presentaron alta viscosidad y contaminación. El proceso de purificación enzimática fue efectivo y permitió mantener una alta masa molar de la fibra y sus estructuras moleculares características (especies con GP3 y GP4). Las muestras comerciales CßG-A y CßG-B mostraron un bajo contenido de ß-glucanos. Finalmente, la CßG-C presentó las mejores propiedades fisicoquímicas y reológicas para su posterior aplicación en alimentos.
Descritores: beta-Glucanas
-Viscosidade
Fibras na Dieta
Alimentos Integrais
Peso Molecular
Limites: Seres Humanos
Tipo de Publ: Artigo Clássico
Responsável: CO56.3 - Biblioteca


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Id: biblio-889234
Autor: Toufiq, Nida; Tabassum, Bushra; Bhatti, Muhammad Umar; Khan, Anwar; Tariq, Muhammad; Shahid, Naila; Nasir, Idrees Ahmad; Husnain, Tayyab.
Título: Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host
Fonte: Braz. j. microbiol;49(2):414-421, Apr.-June 2018. tab, graf.
Idioma: en.
Resumo: Abstract Agricultural crops suffer many diseases, including fungal and bacterial infections, causing significant yield losses. The identification and characterisation of pathogenesis-related protein genes, such as chitinases, can lead to reduction in pathogen growth, thereby increasing tolerance against fungal pathogens. In the present study, the chitinase I gene was isolated from the genomic DNA of Barley (Hordeum vulgare L.) cultivar, Haider-93. The isolated DNA was used as template for the amplification of the ∼935 bp full-length chitinase I gene. Based on the sequence of the amplified gene fragment, class I barley chitinase shares 93% amino acid sequence homology with class II wheat chitinase. Interestingly, barley class I chitinase and class II chitinase do not share sequence homology. Furthermore, the amplified fragment was expressed in Escherichia coli Rosetta strain under the control of T7 promoter in pET 30a vector. Recombinant chitinase protein of 35 kDa exhibited highest expression at 0.5 mM concentration of IPTG. Expressed recombinant protein of 35 kDa was purified to homogeneity with affinity chromatography. Following purification, a Western blot assay for recombinant chitinase protein measuring 35 kDa was developed with His-tag specific antibodies. The purified recombinant chitinase protein was demonstrated to inhibit significantly the important phytopathogenic fungi Alternaria solani, Fusarium spp, Rhizoctonia solani and Verticillium dahliae compared to the control at concentrations of 80 µg and 200 µg.
Descritores: Antifúngicos/farmacologia
Quitinases/farmacologia
Hordeum/enzimologia
Proteínas Recombinantes/metabolismo
-Antifúngicos/química
Antifúngicos/isolamento & purificação
Western Blotting
Quitinases/química
Quitinases/genética
Quitinases/isolamento & purificação
Cromatografia de Afinidade
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Hordeum/genética
Peso Molecular
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Homologia de Sequência de Aminoácidos
Responsável: BR1.1 - BIREME


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Id: biblio-872583
Autor: Fernandes, Liana Bastos Freitas; Rundegren, Jan; Arnebrant, Thomas; Glantz, Per-Olaf.
Título: Characterization of the binding of delmopinol to salivary precipitates / Caracterização da associação de delmopinol com precipitados salivares
Fonte: Braz. dent. j;12(3):173-177, set.-dez. 2001. ilus.
Idioma: en.
Resumo: O objetivo do trabalho é determinar a quantidade de delmopinol associado com cada componente salivar de diferente peso molecular. Saliva não estimulada foi coletada com cinco indivíduos e misturada com delmopinol radioativo obtendo-se uma concentração final de 9,7 mM. As misturas de saliva e delmopinol foram analisadas com eletroforese tanto para o pelete como para o supernatante. Cada amostra foi analisada três vezes em eletroforese. A primeira foi corada com corante de prata. A segunda amostra foi preparada para fazer uma auto-radiografia. A terceira fileira foi cortada em pedaços iguais dissolvidos e analisados com cintilografia. O resultado de cintilografia demonstrou que um grande nível de radioatividade foi detectado em alto peso molecular (600-700 kDa). Em todas as amostras dos peletes foram encontradas grandes quantidades de delmopinol. O resultado da auto-radiografia confirmou que o delmopinol interagiu com proteínas de alto peso molecular (600-700 kDa)
Descritores: Depósitos Dentários/metabolismo
Morfolinas
Proteínas e Peptídeos Salivares/metabolismo
-Autorradiografia
Eletroforese em Gel de Poliacrilamida
Peso Molecular
Ligação Proteica
Saliva
Contagem de Cintilação
Limites: Seres Humanos
Adulto
Meia-Idade
Responsável: BR1.1 - BIREME


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Id: lil-775118
Autor: Sethi, Bijay Kumar; Nanda, Prativa Kumari; Sahoo, Santilata.
Título: Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10
Fonte: Braz. j. microbiol;47(1):143-149, Jan.-Mar. 2016. tab, graf.
Idioma: en.
Projeto: UGC-RGNF Scheme.
Resumo: Abstract Enzyme production by Aspergillus terreus NCFT 4269.10 was studied under liquid static surface and solid-state fermentation using mustard oil cake as a substrate. The maximum lipase biosynthesis was observed after incubation at 30 °C for 96 h. Among the domestic oils tested, the maximum lipase biosynthesis was achieved using palm oil. The crude lipase was purified 2.56-fold to electrophoretic homogeneity, with a yield of 8.44%, and the protein had a molecular weight of 46.3 kDa as determined by SDS-PAGE. Enzyme characterization confirmed that the purified lipase was most active at pH 6.0, temperature of 50 °C, and substrate concentration of 1.5%. The enzyme was thermostable at 60 °C for 1 h, and the optimum enzyme–substrate reaction time was 30 min. Sodium dodecyl sulfate and commercial detergents did not significantly affect lipase activity during 30-min incubation at 30 °C. Among the metal ions tested, the maximum lipase activity was attained in the presence of Zn2+, followed by Mg2+ and Fe2+. Lipase activity was not significantly affected in the presence of ethylenediaminetetraacetic acid, sodium lauryl sulfate and Triton X-100. Phenylmethylsulfonyl fluoride (1 mM) and the reducing, β-mercaptoethanol significantly inhibited lipase activity. The remarkable stability in the presence of detergents, additives, inhibitors and metal ions makes this lipase unique and a potential candidate for significant biotechnological exploitation.
Descritores: Aspergillus/enzimologia
Lipase/metabolismo
-Cátions Bivalentes/metabolismo
Eletroforese em Gel de Poliacrilamida
Estabilidade Enzimática
Ativadores de Enzimas/análise
Inibidores Enzimáticos/análise
Concentração de Íons de Hidrogênio
Lipase/química
Lipase/isolamento & purificação
Peso Molecular
Mercaptoetanol/metabolismo
Metais/metabolismo
Temperatura Ambiente
Responsável: BR1.1 - BIREME


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Id: lil-769668
Autor: Naz, Sehar Afshan; Jabeen, Nusrat; Sohail, Muhammad; Rasool, Sheikh Ajaz.
Título: Biophysicochemical characterization of Pyocin SA189 produced by Pseudomonas aeruginosa SA189
Fonte: Braz. j. microbiol;46(4):1147-1154, Oct.-Dec. 2015. tab, graf.
Idioma: en.
Resumo: Abstract Pseudomonas aeruginosa, in spite of being a ubiquitous organism (as it is found in soil, water, and humans), is also an opportunistic pathogen. In order to maintain its diversity in the community, it produces various toxic proteins, known as, bacteriocins. In the present study, pyocin SA189, which is a bacteriocin produced by P. aeruginosa SA189 (isolated from a clinical sample) was characterized. P. aeruginosa SA189, as identified by the conventional and 16S rRNA gene amplification, produced pyocin SA189 of molecular weight of 66 k Da. The pyocin showed antimicrobial activity against several clinically relevant Gram-positive and Gram-negative bacteria and was substantially stable for wide ranges of temperature and pH. Furthermore, the pyocin also retained its biological activity upon treatment with metal ions, organic solvents, and various proteolytic and lipolytic enzymes. The data from the growth kinetics indicated that the maximum bacteriocin production occurred in the late log phase. Overall, our results signify the potential of pyocin SA189 as a bio-control agent.
Descritores: Pseudomonas aeruginosa/metabolismo
Piocinas/isolamento & purificação
-DNA Bacteriano/química
DNA Bacteriano/genética
DNA Ribossômico/química
DNA Ribossômico/genética
Especificidade de Hospedeiro
Concentração de Íons de Hidrogênio
Peso Molecular
Pseudomonas aeruginosa/genética
Piocinas/química
/genética
RNA, RIBOSOMAL, ABNORMALITIES, MULTIPLES/genética
Análise de Sequência de DNA
Temperatura Ambiente
Responsável: BR1.1 - BIREME


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Id: lil-749712
Autor: Hongming, Liu; Xu, Lou; Zhaojian, Ge; Fan, Yang; Dingbin, Chen; Jianchun, Zhu; Jianhong, Xu; Shunpeng, Li; Qing, Hong.
Título: Isolation of an aryloxyphenoxy propanoate (AOPP) herbicide-degrading strain Rhodococcus ruber JPL-2 and the cloning of a novel carboxylesterase gene (feh)
Fonte: Braz. j. microbiol;46(2):425-432, Apr-Jun/2015. tab, graf.
Idioma: en.
Projeto: The National High Technology Research and Development Program of China; . Chinese National Natural Science Fund; . Chinese National Natural Science Fund; . Science and Technology of Jiangsu Province.
Resumo: The strain JPL-2, capable of degrading fenoxaprop-P-ethyl (FE), was isolated from the soil of a wheat field and identified as Rhodococcus ruber. This strain could utilize FE as its sole carbon source and degrade 94.6% of 100 mg L−1 FE in 54 h. Strain JPL-2 could also degrade other aryloxyphenoxy propanoate (AOPP) herbicides. The initial step of the degradation pathway is to hydrolyze the carboxylic acid ester bond. A novel esterase gene feh, encoding the FE-hydrolyzing carboxylesterase (FeH) responsible for this initial step, was cloned from strain JPL-2. Its molecular mass was approximately 39 kDa, and the catalytic efficiency of FeH followed the order of FE > quizalofop-P-ethyl > clodinafop-propargyl > cyhalofop-butyl > fluazifop-P-butyl > haloxyfop-P-methyl > diclofop-methy, which indicated that the chain length of the alcohol moiety strongly affected the hydrolysis activity of the FeH toward AOPP herbicides.
Descritores: Carboxilesterase/genética
Carboxilesterase/metabolismo
Herbicidas/metabolismo
Oxazóis/metabolismo
Propionatos/metabolismo
Rhodococcus/isolamento & purificação
Rhodococcus/metabolismo
-Biotransformação
Clonagem Molecular
Análise por Conglomerados
Carboxilesterase/química
DNA Bacteriano/química
DNA Bacteriano/genética
DNA Ribossômico/química
DNA Ribossômico/genética
Dados de Sequência Molecular
Peso Molecular
Filogenia
/genética
RNA, RIBOSOMAL, ABNORMALITIES, MULTIPLES/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Rhodococcus/enzimologia
Rhodococcus/genética
Análise de Sequência de DNA
Microbiologia do Solo
Especificidade por Substrato
Triticum/crescimento & desenvolvimento
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-748256
Autor: Gomaa, Ola M.; Momtaz, Osama A..
Título: Copper induction and differential expression of laccase in Aspergillus flavus
Fonte: Braz. j. microbiol;46(1):285-292, 05/2015. tab, graf.
Idioma: en.
Resumo: Aspergillus flavus was isolated from soil and exhibited laccase activity under both constitutive and copper induced conditions. Spiking the medium with 1 mM copper sulfate resulted in an increase in the activity which reached 51.84 U/mL, a distinctive protein band was detected at 60 kDa. The extracellular enzyme was purified 81 fold using gel filtration chromatography and resulted in two different laccase fractions L1 and L2, the latter had a higher enzymatic activity which reached 79.57 U/mL and specific activity of 64.17 U/μg protein. The analysis of the spectrum of the L2 fraction showed a shoulder at 330 nm which is characteristic for T2/T3 copper centers; both copper and zinc were detected suggesting that this is an unconventional white laccase. Primers of laccase gene were designed and synthesized to recover specific gene from A. flavus. Sequence analysis indicated putative laccase (Genbank ID: JF683612) at the amino acid level suggesting a close identity to laccases from other genera containing the copper binding site. Decolorization of textile waste water under different conditions showed possible application in bioremediation within a short period of time. The effect of copper on A. flavus was concentration dependent.
Descritores: Aspergillus flavus/efeitos dos fármacos
Aspergillus flavus/enzimologia
Cobre/metabolismo
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Lacase/biossíntese
Ativação Transcricional/efeitos dos fármacos
-Aspergillus flavus/genética
Aspergillus flavus/isolamento & purificação
Cromatografia em Gel
Meios de Cultura/química
DNA Fúngico/genética
Eletroforese em Gel de Poliacrilamida
Resíduos Industriais
Lacase/química
Lacase/isolamento & purificação
Dados de Sequência Molecular
Peso Molecular
Análise de Sequência de DNA
Homologia de Sequência de Aminoácidos
Microbiologia do Solo
Análise Espectral
Purificação da Água
Responsável: BR1.1 - BIREME



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