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Id: lil-772699
Autor: Alarcón C, Oscar M; Giménez, Esther.
Título: Cambios en la actividad de algunas enzimas séricas en ratas con hipervitaminosis E / Changes in activity of some serum enzymes in rats with hypervitaminosis E
Fonte: Rev. Inst. Nac. Hig;45(1):7-13, jun. 2014. tab.
Idioma: es.
Resumo: Poco se sabe sobre los cambios en la actividad de las enzimas séricas relacionadas con la función hepática durante la hipervitaminosis E. En el presente trabajo se estudió el efecto de la administración intraperitoneal de 50, 100, 200 y 400 mg de vitamina E/día, durante 20 días sobre la actividad enzimática sérica en 60 ratas Wistar machos, de 12 semanas de edad, con pesos entre 180 y 200 gramos. El grupo control estuvo integrado por 15 ratas Wistar sanas, con edad y peso similares a los animales tratados. Al final del estudio, se tomaron muestras de sangre para la determinación de la vitamina E y la actividad de las enzimas: alanina aminotransferasa (ALT), aspartato aminotransferasa (AST), α-amilasa (AMS), arginasa (ARG), fosfohexosaisomerasa (PHI), fosfatasa alcalina (ALP), γ-glutamiltransferasa (γ-GT) y 5´-nucleotidasa (5´-N). La administración de vitamina E en exceso incrementó de manera significativa (p<0,05) el contenido sérico de la vitamina E y la actividad de todas las enzimas valoradas (p< 0,05); mientras que la α-amilasa disminuyó (p< 0,05) al ser comparada con los controles no tratados. Nuestros resultados proporcionan evidencia que la administración a corto plazo de dosis altas de vitamina E, produce un incremento en la actividad de las enzimas marcadoras de daño hepático (como aminotransferasas, ARG y PHI) y de colestasis (como ALP, 5´-N y γ-GT), que se corresponde con la forma mixta de enfermedad hepática (daño+colestasis).

Little is known about the possible changes in blood enzyme activity related to liver function during hypervitaminosis E. In the present work the effects of intraperitoneal administration of 50, 100, 200 and 400 mg of vitamin E (α-tocopherol) daily for 20 days, respectively, on the serum enzyme activity in 60 white male Wistar rats, aged 12 weeks and weighing 180-200 g, were studied. The group control was integrated by 15 healthy rats with similar characteristics (age and weight) to treated animals. Excess of vitamin E produced a significant (p<0.05) increase in the serum content of vitamin E and in the activity (p<0.05) of the following enzymes: alanine aminotransferase (ALT), aspartate aminotransferase (AST), arginase (ARG), phosphohexosaisomerase (PHI), alkaline phosphatase (ALP), γ-glutamyltransferase (γ-GT) and 5´-nucleotidase (5´-N) while α-amylase (AMS) decreased (p<0.05) on comparing with the control group. These changes depend on the doses given of vitamin E. In conclusion, our results provide evidence that short-term administration of high doses of vitamin E produces an increase in the activity of the enzymes marker of liver damage (as aminotransferases, ARG and PHI) and of cholestasis (as ALP, γ-GT and 5´-N) that correspond to the mixed form of liver disease (injury+cholestasis).
Descritores: Vitamina E/administração & dosagem
Ratos Wistar/metabolismo
Ativadores de Enzimas
alfa-Tocoferol
-Saúde Pública
Transaminases/análise
Infusões Parenterais/métodos
Limites: Animais
Masculino
Ratos
Tipo de Publ: 57800
Responsável: VE9.1 - Biblioteca


  2 / 28 LILACS  
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Id: lil-775124
Autor: Coelho, Sheila Lorena de Araújo; Magalhães, Valter Cruz; Marbach, Phellippe Arthur Santos; Cazetta, Marcia Luciana.
Título: A new alkalophilic isolate of Bacillus as a producer of cyclodextrin glycosyltransferase using cassava flour
Fonte: Braz. j. microbiol;47(1):120-128, Jan.-Mar. 2016. tab, graf.
Idioma: en.
Resumo: Abstract Cyclodextrin glycosyltransferase (CGTase) catalyzes the conversion of starch into non-reducing cyclic sugars, cyclodextrins, which have several industrial applications. This study aimed to establish optimal culture conditions for β-CGTase production by Bacillus sp. SM-02, isolated from soil of cassava industries waste water lake. The optimization was performed by Central Composite Design (CCD) 2, using cassava flour and corn steep liquor as substrates. The maximum production of 1087.9 U mL−1 was obtained with 25.0 g L−1 of cassava flour and 3.5 g L−1 of corn steep after 72 h by submerged fermentation. The enzyme showed optimum activity at pH 5.0 and temperature 55 °C, and maintained thermal stability at 55 °C for 3 h. The enzymatic activity was stimulated in the presence of Mg+2, Ca+2, EDTA, K+, Ba+2 and Na+ and inhibited in the presence of Hg+2, Cu+2, Fe+2 and Zn+2. The results showed that Bacillus sp. SM-02 have good potential for β-CGTase production.
Descritores: Bacillus/isolamento & purificação
Bacillus/metabolismo
Meios de Cultura/química
Glucosiltransferases/metabolismo
-Ativadores de Enzimas/metabolismo
Inibidores Enzimáticos/análise
Concentração de Íons de Hidrogênio
Manihot/metabolismo
Microbiologia do Solo
Temperatura Ambiente
Zea mays/metabolismo
Responsável: BR1.1 - BIREME


  3 / 28 LILACS  
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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


  4 / 28 LILACS  
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Id: lil-723134
Autor: Farrokh, Parisa; Yakhchali, Bagher; Asghar Karkhane, Ali.
Título: Cloning and characterization of newly isolated lipase from Enterobacter sp. Bn12
Fonte: Braz. j. microbiol;45(2):677-687, Apr.-June 2014. ilus, graf, tab.
Idioma: en.
Resumo: A mesophilic Enterobacter sp. Bn12 producing an alkaline thermostable lipase was isolated from soil in Tehran, Iran. The lipase gene (ELBn12) was identified from a genomic library. Sequence analysis of the DNA fragment revealed an open reading frame of 879 bp encoding a lipase with a molecular mass of 31.3 kDa. The deduced amino acid sequence showed 96% identity with a lipase of Enterobacter sp. Ag1 and the identity of their DNA sequences was 88.9%. ELBn12 belongs to the lipase subfamily I.1 and its catalytic triad consists of Ser82, Asp237 and His259. The lipase was expressed in Escherichia coli (BL21) pLysS and partially purified by anion exchange chromatography. The maximum activity of ELBn12 was obtained at temperature of 60 °C and pH 8.0 towards tricaprylin (C8) and its specific activity was around 2900 U/mg. ELBn12 was stable within a broad pH range from 6.0 to 11.0. The enzyme showed high stability in both polar and nonpolar organic solvents at 50% (v/v). The lipase activity was enhanced in the presence of 10 mM of Ca2+, Mg2+ and K+, while heavy metals (Fe3+ and Zn2+) had strong inhibitory effect. ELBn12 showed high activity in the presence of 1% (w/v) nonionic surfactants, however ionic surfactants inhibited the lipolytic activity. ELBn12 characteristics show that it has a potential to be used in various industrial processes.
Descritores: Enterobacter/enzimologia
Lipase/isolamento & purificação
Lipase/metabolismo
-Sequência de Aminoácidos
Técnicas de Tipagem Bacteriana
Sequência de Bases
Cromatografia por Troca Iônica
Clonagem Molecular
DNA Bacteriano/química
DNA Bacteriano/genética
Estabilidade Enzimática
Enterobacter/classificação
Enterobacter/genética
Enterobacter/isolamento & purificação
Ativadores de Enzimas/análise
Inibidores Enzimáticos/análise
Escherichia coli/genética
Expressão Gênica
Concentração de Íons de Hidrogênio
Irã (Geográfico)
Lipase/química
Lipase/genética
Dados de Sequência Molecular
Peso Molecular
Fases de Leitura Aberta
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Análise de Sequência de DNA
Homologia de Sequência de Aminoácidos
Homologia de Sequência do Ácido Nucleico
Microbiologia do Solo
Temperatura Ambiente
Responsável: BR1.1 - BIREME


  5 / 28 LILACS  
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Id: lil-709465
Autor: Yehia, Ramy Sayed.
Título: Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
Fonte: Braz. j. microbiol;45(1):127-134, 2014. ilus, graf, tab.
Idioma: en.
Resumo: Manganese peroxidase (MnP) was produced from white rot edible mushroom Pleurotus ostreatus on the culture filtrate. The enzyme was purified to homogeneity using (NH4)2SO4 precipitation, DEAE-Sepharose and Sephadex G-100 column chromatography. The final enzyme activity achieved 81UmL-1, specific activity 78 U mg-1 with purification fold of 130 and recovery 1.2% of the crude enzyme. SDS-PAGE indicated that the pure enzyme have a molecular mass of approximately 42 kDa. The optimum pH was between 4-5 and the optimum temperature was 25 ºC. The pure MnP activity was enhanced by Mn2+,Cu2+,Ca2+ and K+ and inhibited by Hg+2 and Cd+2.H2O2 at 5 mM enhanced MnP activity while at 10 mM inhibited it significantly. The MnP-cDNA encoding gene was sequenced and determined (GenBank accession no. AB698450.1). The MnP-cDNA was found to consist of 497 bp in an Open Reading Frame (ORF) encoding 165 amino acids. MnP from P. ostreatus could detoxify aflatoxin B1 (AFB1) depending on enzyme concentration and incubation period. The highest detoxification power (90%) was observed after 48 h incubation at 1.5 U mL-1 enzyme activities.
Descritores: Aflatoxinas/metabolismo
Peroxidases/isolamento & purificação
Peroxidases/metabolismo
Pleurotus/enzimologia
-Biotransformação
Precipitação Química
Cromatografia em Gel
Cromatografia por Troca Iônica
DNA Fúngico/química
DNA Fúngico/genética
Eletroforese em Gel de Poliacrilamida
Ativadores de Enzimas/metabolismo
Inibidores Enzimáticos/metabolismo
Concentração de Íons de Hidrogênio
Dados de Sequência Molecular
Peso Molecular
Metais/metabolismo
Fases de Leitura Aberta
Peroxidases/química
Análise de Sequência de DNA
Temperatura Ambiente
Responsável: BR1.1 - BIREME


  6 / 28 LILACS  
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Id: lil-705271
Autor: Bisht, Deepali; Yadav, Santosh Kumar; Darmwal, Nandan Singh.
Título: An oxidant and organic solvent tolerant alkaline lipase by P. aeruginosa mutant: downstream processing and biochemical characterization
Fonte: Braz. j. microbiol;44(4):1305-1314, Oct.-Dec. 2013. ilus, tab.
Idioma: en.
Resumo: An extracellular alkaline lipase from Pseudomonas aeruginosa mutant has been purified to homogeneity using acetone precipitation followed by anion exchange and gel filtration chromatography and resulted in 27-fold purification with 19.6% final recovery. SDS-PAGE study suggested that the purified lipase has an apparent molecular mass of 67 kDa. The optimum temperature and pH for the purified lipase were 45°C and 8.0, respectively. The enzyme showed considerable stability in pH range of 7.0-11.0 and temperature range 35-55 °C. The metal ions Ca2+, Mg2+ and Na+ tend to increase the enzyme activity, whereas, Fe2+ and Mn2+ ions resulted in discreet decrease in the activity. Divalent cations Ca+2 and Mg+2 seemed to protect the enzyme against thermal denaturation at high temperatures and in presence of Ca+2 (5 mM) the optimum temperature shifted from 45°C to 55°C. The purified lipase displayed significant stability in the presence of several hydrophilic and hydrophobic organic solvents (25%, v/v) up to 168 h. The pure enzyme preparation exhibited significant stability and compatibility with oxidizing agents and commercial detergents as it retained 40-70% of its original activities. The values of Km and Vmax for p-nitrophenyl palmitate (p-NPP) under optimal conditions were determined to be 2.0 mg.mL-1 and 5000 μg.mL-1.min-1, respectively.
Descritores: Lipase/metabolismo
Pseudomonas aeruginosa/enzimologia
-Precipitação Química
Cromatografia em Gel
Cromatografia por Troca Iônica
Cátions/metabolismo
Ativadores de Enzimas
Estabilidade Enzimática
Inibidores Enzimáticos/metabolismo
Concentração de Íons de Hidrogênio
Cinética
Lipase/química
Lipase/isolamento & purificação
Metais/metabolismo
Oxidantes/metabolismo
Pseudomonas aeruginosa/genética
Solventes/metabolismo
Temperatura Ambiente
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  7 / 28 LILACS  
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Id: lil-688598
Autor: Gomaa, Eman Zakaria.
Título: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes
Fonte: Braz. j. microbiol;44(2):529-537, 2013. graf, tab.
Idioma: en.
Resumo: The potentiality of 23 bacterial isolates to produce alkaline protease and carboxymethyl-cellulase (CMCase) on Ficus nitida wastes was investigated. Bacillus pumillus ATCC7061 was selected as the most potent bacterial strain for the production of both enzymes. It was found that the optimum production of protease and CMCase were recorded at 30 °C, 5% Ficus nitida leaves and incubation period of 72 h. The best nitrogen sources for protease and CMCase production were yeast extract and casein, respectively. Also maximum protease and CMCase production were reported at pH 9 and pH 10, respectively. The enzymes possessed a good stability over a pH range of 8-10, expressed their maximum activities at pH10 and temperature range of 30-50 °C, expressed their maximum activities at 50 °C. Ions of Hg2+, Fe2+ and Ag+ showed a stimulatory effect on protease activity and ions of Fe2+, Mg2+, Ca2+, Cu2+ and Ag+ caused enhancement of CMCase activity. The enzymes were stable not only towards the nonionic surfactants like Triton X-100 and Tween 80 but also the strong anionic surfactant, SDS. Moreover, the enzymes were not significantly inhibited by EDTA or cystein. Concerning biotechnological applications, the enzymes retained (51-97%) of their initial activities upon incubation in the presence of commercials detergents for 1 h. The potential use of the produced enzymes in the degradation of human hair and cotton fabric samples were also assessed.
Descritores: Bacillus/enzimologia
Bacillus/crescimento & desenvolvimento
Proteínas de Bactérias/metabolismo
Carboximetilcelulose Sódica/metabolismo
Endopeptidases/metabolismo
Ficus/microbiologia
Resíduos Industriais
-Proteínas de Bactérias/química
Carboximetilcelulose Sódica/química
Estabilidade Enzimática
Endopeptidases/química
Ativadores de Enzimas/metabolismo
Concentração de Íons de Hidrogênio
Metais/metabolismo
Temperatura Ambiente
Fatores de Tempo
Responsável: BR1.1 - BIREME


  8 / 28 LILACS  
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Id: lil-665847
Autor: Kumar, Sumit; Karan, Ram; Kapoor, Sanjay; Singh, S P; Khare, S K.
Título: Screening and isolation of halophilic bacteria producing industrially important enzymes
Fonte: Braz. j. microbiol;43(4):1595-1603, Oct.-Dec. 2012. graf, tab.
Idioma: en.
Resumo: Halophiles are excellent sources of enzymes that are not only salt stable but also can withstand and carry out reactions efficiently under extreme conditions. The aim of the study was to isolate and study the diversity among halophilic bacteria producing enzymes of industrial value. Screening of halophiles from various saline habitats of India led to isolation of 108 halophilic bacteria producing industrially important hydrolases (amylases, lipases and proteases). Characterization of 21 potential isolates by morphological, biochemical and 16S rRNA gene analysis found them related to Marinobacter, Virgibacillus, Halobacillus, Geomicrobium, Chromohalobacter, Oceanobacillus, Bacillus, Halomonas and Staphylococcus genera. They belonged to moderately halophilic group of bacteria exhibiting salt requirement in the range of 3-20%. There is significant diversity among halophiles from saline habitats of India. Preliminary characterization of crude hydrolases established them to be active and stable under more than one extreme condition of high salt, pH, temperature and presence of organic solvents. It is concluded that these halophilic isolates are not only diverse in phylogeny but also in their enzyme characteristics. Their enzymes may be potentially useful for catalysis under harsh operational conditions encountered in industrial processes. The solvent stability among halophilic enzymes seems a generic novel feature making them potentially useful in non-aqueous enzymology.
Descritores: Ativadores de Enzimas/análise
Biodiversidade
Halobacteriales/isolamento & purificação
Hidrolases/análise
Hidrolases/isolamento & purificação
Solventes/análise
-Catálise
Microbiologia Ambiental
Métodos
Tipo de Publ: Estudo Comparativo
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica


  9 / 28 LILACS  
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Id: lil-665837
Autor: Behera, Shuvashish; Mohanty, Rama C; Ray, Ramesh C.
Título: Ethanol fermentation of sugarcane molasses by Zymomonas mobilis MTCC 92 immobilized in Luffa cylindrica L. sponge discs and Ca-alginate matrices
Fonte: Braz. j. microbiol;43(4):1499-1507, Oct.-Dec. 2012. graf, tab.
Idioma: en.
Projeto: UGC.
Resumo: Bio-ethanol production from cane molasses (diluted to 15 % sugar w/v) was studied using the bacterium, Zymomonas mobilis MTCC 92 entrapped in luffa (Luffa cylindrica L.) sponge discs and Ca-alginate gel beads as the immobilizing matrices. At the end of 96 h fermentation, the final ethanol concentrations were 58.7 ± 0.09 and 59.1 ± 0.08 g/l molasses with luffa and Ca-alginate entrapped Z. mobilis cells, respectively exhibiting 83.25 ± 0.03 and 84.6 ± 0.02 % sugar conversion. There was no statistical significant difference (Fischer's LSD) in sugar utilization (t = 0.254, p <0.801) and ethanol production (t =-0.663, p <0.513) between the two immobilization matrices used. Further, the immobilized cells in both the matrices were physiologically active for three more cycles of operation with less than 15 % decrease in ethanol yield in the 4th cycle, which was due to some leakage of cells. In conclusion, luffa sponge was found to be equally good as Ca-alginate as a carrier material for bacterial (Z. mobilis. cell immobilization for ethanol production. Further, it has added advantages such as it is cheap, non-corrosive and has no environmental hazard.
Descritores: Ativadores de Enzimas
Etanol/análise
Fermentação
Luffa/crescimento & desenvolvimento
Melaço/análise
Zymomonas/isolamento & purificação
-Células Imobilizadas
Métodos
Tipo de Publ: Estudo Comparativo
Estudos de Avaliação
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica


  10 / 28 LILACS  
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Id: lil-622828
Autor: Cai, Shuang-Hu; Wu, Zao-He; Jian, Ji-Chang; Lu, Yi-Shan; Tang, Ju-Feng.
Título: Characterization of pathogenic Aeromonas veronii bv. veronii associated with ulcerative syndrome from Chinese longsnout catfish (Leiocassis longirostris Günther)
Fonte: Braz. j. microbiol;43(1):382-388, Jan.-Mar. 2012. ilus, tab.
Idioma: en.
Resumo: 273 bacterial strains were isolated from 20 Chinese longsnout catfish samples. The biochemical characteristics of all strains conformed to the species description of Aeromonas veronii bv. veronii on the basis of Vitek GNI+ card. Furthermore, 16S rDNA, gyrB and rpoD sequences of the representative strain PY50 were sequenced and showed high similarity with A. veronii bv. veronii in Genbank. Antibiotic-resistance of the representative strain PY50 was assessed by the Kirby-Bauer disk diffusion method, and the results showed it was susceptible and moderately susceptible to 13 and 4 of the 21 antimicrobial agents tested. Extracellular products of strain PY50 contained gelatinase, lecithinase, elastase, most of lipase and lipopolysaccharide. Virulence of strain PY50 and extracellular products to Chinese longsnout catfish were also tested, and LD50 were about 3.47~10(4) CFU per fish and 11.22 ƒÊg per fish in intraperitoneal injection respectively. This is the first report that A. veronii bv. veronii was the pathogenic agent of ulcerative syndrome in Chinese longsnout catfish.
Descritores: Aeromonas/isolamento & purificação
Aeromonas/patogenicidade
Antibacterianos/análise
Ativadores de Enzimas/análise
Peixes-Gato/genética
Peixes-Gato/microbiologia
-Amostras de Alimentos
Limites: Animais
Tipo de Publ: Estudo Comparativo
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica



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