Base de dados : LILACS
Pesquisa : E05.196.401.402.236 [Categoria DeCS]
Referências encontradas : 4 [refinar]
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Id: lil-656691
Autor: López, Ruth; Monteón, Víctor; Chan, Ernesto; Montejo, Rubí; Chan, Manuel.
Título: Oxygen limitation favors the production of protein with antimicrobial activity in Pseudoalteromonas sp
Fonte: Braz. j. microbiol;43(3):1206-1212, July-Sept. 2012. ilus, graf.
Idioma: en.
Resumo: This study examined the effect of dissolved oxygen concentration on the production of biomass and metabolites with antimicrobial activity of Pseudoalteromonas sp cultured at 0, 150, 250, or 450 revolutions per minute (rev. min-1). Dissolved oxygen (D.O) was monitored during the fermentation process, biomass was quantified by dry weight, and antimicrobial activity was assessed using the disk diffusion method. The bacterium Pseudoalteromonas reached similar concentration of biomass under all experimental agitation conditions, whereas antimicrobial activity was detected at 0 and 150 rev. min-1 registering 0% and 12% of D.O respectively corresponding to microaerophilic conditions. Antibiotic activity was severely diminished when D.O was above 20% of saturation; this corresponded to 250 or 450 rev. min-1. SDS-PAGE electrophoresis revealed a protein with a molecular weight of approximately 80 kilodaltons (kDa) with antimicrobial activity. Pseudoalteromonas is capable of growing under oxic and microaerophilic conditions but the metabolites with antimicrobial activity are induced under microaerophilic conditions. The current opinion is that Pseudoalteromonas are aerobic organisms; we provide additional information on the amount of dissolved oxygen during the fermentation process and its effect on antimicrobial activity.
Descritores: Antibacterianos/análise
Biomassa
Fermentação
Metabolismo
Oxigênio/metabolismo
Pseudoalteromonas/metabolismo
-Eletroforese Descontínua
Bactérias Aeróbias Gram-Negativas
Métodos
Técnicas
Tipo de Publ: Estudo de Avaliação
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica


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Id: lil-656680
Autor: Das, Arpan; Ghosh, Uma; Mohapatra, Pradeep Kumar Das; Pati, Bikas Ranjan; Mondal, Keshab Chandra.
Título: Study on Thermodynamics and Adsorption kinetics of Purified endoglucanase (CMCase) from Penicillium notatum NCIM NO-923 produced under mixed solid-state fermentation of waste cabbage and Bagasse
Fonte: Braz. j. microbiol;43(3):1103-1111, July-Sept. 2012. ilus, graf, tab.
Idioma: en.
Resumo: In the current study, one thermostable endoglucanase was purified from Penicillium notatum NCIM NO-923 through mixed solid state fermentation of waste cabbage and bagasse. The molecular weight of the purified enzyme was 55kDa as determined by SDS polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme had low activation energy (Ea) of 36.39KJ mol-1 for carboxymethyl cellulose hydrolysis and the enthalpy and entropy for irreversible inactivation was 87 kJ mol −1 and 59.3 J mol −1 K−1 respectively. The enzyme was quite thermostable with a Tm value of 62.2˚C. The pKa1 and pKa2 of ionizable groups of the active sites were 2.5 and 5.3 respectively. Apparent Km, Vmax and Kcat of the enzyme were found to be 5.2 mg mL-1, 80 U/gds and 322.4 sec-1 respectively. The enzyme showed about 1.4 fold increased activity in presence of 10mM MgSO4. Adsorption of endoglucanase on Avicel at wide pH range was studied at different temperatures. Langmuir type adsorption isotherm at 10˚C showed maximum adsorption strength of enzyme at pH 3.0, which was in a range of optimum pH of the enzyme.
Descritores: Brassica
Celulase/análise
Entropia
Ativação Enzimática
Fermentação
Isoterma
Penicillium chrysogenum/isolamento & purificação
-Eletroforese Descontínua
Amostras de Alimentos
Hidrólise
Microbiologia Industrial
Limites: Humanos
Tipo de Publ: Estudo Comparativo
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica


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Id: lil-340481
Autor: Losso, Estela Maris; Nicolau, José.
Título: Lactate dehydrogenase isoenzymes in dental pulp of rats according to stage of root development
Fonte: Braz. dent. j;14(1):5-11, June 2003. tab, graf.
Idioma: en.
Resumo: The objective of this study was to present a classification of the root development stage of female rat molar teeth and to evaluate the variation in the lactate dehydrogenase (LDH) activity and electrophoretic isoenzyme profile according to the stage of root development of the molar teeth. We also studied the LDH activity and isoenzymes of the pulp of incisor teeth. The stage of development of the rat first molar at the age of 15 days and that of the second molar at the age of 18 days was classified as the beginning of root formation. At the age of 15 days, the electrophoretic profile of the isoenzymes for the first molar showed a prevalence of LDH-1 followed by LDH-2. However, for the maxillary second molar there was a prevalence of LDH-4 followed by LDH-1, while for the mandibular second molar LDH-1 predominated followed by LDH-2 and LDH-4. From 18 days of age, the prevalence was always of LDH-1. The electrophoretic profile of LDH isoenzymes from the pulp of the incisor teeth at the ages studied (25 and 60 days) showed the following order of prevalence: LDH-1 > LDH-2 > LDH-3 > LDH-4 > LDH-5. These results suggest that there are variations in the prevalence of the various forms of LDH isoenzymes in the dental pulp of rats according to the developmental stage of the root
Descritores: Polpa Dentária/enzimologia
Isoenzimas/análise
L-Lactato Desidrogenase/análise
Odontogênese/fisiologia
Raiz Dentária/crescimento & desenvolvimento
-Fatores Etários
Dentinogênese/fisiologia
Eletroforese Descontínua
Eletroforese em Gel de Poliacrilamida
Incisivo/crescimento & desenvolvimento
Dente Molar/crescimento & desenvolvimento
Ratos Wistar
Estatística como Assunto
Limites: Animais
Feminino
Ratos
Responsável: BR1.1 - BIREME


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Id: lil-134606
Autor: Ramos, P. R. R; Urtado, S. L. R; Almeida, M. R. H; Bortolozzi, J.; Silva, E. T.
Título: An improved electrophoretic method for the determination of serum milk protein variants in Gyr-Holstein cows
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;25(11):1107-12, 1992. ilus.
Idioma: en.
Resumo: Milk serum proteins such as alpha-lactalbumin (ALA) and beta-lactoglobulin (BLG) present biochemical polymorphism which is under the control of codominant autosomal alleles. In the present report, we propose modifications of traditional electrophoretic techniques such as increasing the running gel concentration from 5 to 10% and the addition of 5 M urea to the stacking gel, which permitted the detection of two variants (A and B) at the ALA and BLG loci. About 8 microliters of milk serum (6 mg/ml protein) and 10 microliters of total fresh milk were applied. Bovine serum albumin (BSA) and immunolactoglobulins (ILG) could also be discriminated. Total fresh milk was as useful as the purified serum milk proteins for the discrimination of ALA and BLG serum milk protein polymorphism by alkaline vertical slab polyacrylamide gel electrophoresis. However, BSA and ILG ran with caseins, which prevented their characterization in this system
Descritores: Eletroforese Descontínua/métodos
Eletroforese em Gel de Poliacrilamida/métodos
Variação Genética
Proteínas do Leite/análise
-Bovinos
Lactalbumina/análise
Lactoglobulinas/análise
Proteínas do Leite/genética
Limites: Animais
Feminino
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR26.1 - Biblioteca Central



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