247 resultados para Ni2


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Fundao de Amparo Pesquisa do Estado de So Paulo (FAPESP)

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Amostra de esmectita pertencente a Serra de Maicuru (Estado do Par, Norte do Brasil, regio amaznica) foi pilarizada com Al<sub>13</sub>, A Argila pilarizada com alumnio (Al-PILC) foi caracterizada por DRX, MEV e EDS. Para a anlise textural foram utilizadas isotermas de adsoro-desoro utilizando o nitrognio. Este artigo dirigido ao estudo da adsoro de metais pesados. A adsoro dos ons de Cu<sup>2+</sup>, Ni<sup>2+</sup>e Co<sup>2+</sup> foi realizadas com a matriz Al-PILC em temperatura ambiente com solues aquosas contendo os ons metlicos. Os modelos de adsoro adotados foram os de Langmuir, Freundlich e Temkin que foram aplicados aos valores obtidos experimentalmente com regresso linear. A equao de Langmuir foi o melhor modelo de linearizao com r = 0,999. A equao de Freundlich apresentou limitaes em altas concentraes, mas foram obtidos valores (K<sub>f</sub> e n) bastante aceitveis utilizando este modelo. Os parmetros foram utilizados para calcular a quantidade de N<sub>f</sub> em funo de Cs.

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Coordenao de Aperfeioamento de Pessoal de Nvel Superior (CAPES)

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Coordenao de Aperfeioamento de Pessoal de Nvel Superior (CAPES)

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Coordenao de Aperfeioamento de Pessoal de Nvel Superior (CAPES)

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Ps-graduao em Cincia dos Materiais - FEIS

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In this study, it was demonstrated that -galactosidase can be deactivated and reactivated with EDTA and divalent metal ions. The enzyme was deactivated after 20 minutes in EDTA solution. Maximal deactivation at the lowest EDTA concentration (10-3 mol.L-1) occurred in the presence of Tris-HCl buffer (pH 7.0). The enzyme recovered 50% of its initial activity after 10 minutes at Mg2+concentrations higher than 0.1 mmol.L-1. Experimental concentrations of 0.1 mmol.L-1 Mn2+ and 1.0 mmol.L-1 Co2+ were sufficient to reactivate the enzyme to around 300% of the control activity for the Mn2+ ion and nearly 100% for the Co2+ ion. The enzyme gradually lost its activity when the Co2+ concentration was 10-2 mol.L-1. Ni2+ and Zn2+ were unable to restore the catalytic activity. Km app and Vmax app were 1.95 0.05 mmol.L-1 and 5.40 0.86x10-2 mmol.min-1.mg-1, with o-NPG as substrate. Optimal temperature and pH were 34oC and 7.5. The half-life (t1/2) at 30C was 17.5 min for the holoenzyme and 11.0 min for the apoenzyme. With respect to pH variation, the apoenzyme proved to be more sensitive than the holoenzyme. Keywords: -galactosidase. Divalent metallic ions. Enzyme activity. Stability. RESUMO Efeito de ons metlicos divalentes na atividade e estabilidade da -galactosidase isolada de Kluyveromyces lactis Este estudo demonstra como a -galactosidase pode ser desativada e reativada usando EDTA e ons metlicos divalentes. A enzima foi desativada aps 20 minutos na presena de EDTA. Desativao mxima para a menor concentrao de EDTA (10-3 mol.L-1) ocorreu na presena do tampo Tris-HCl. A enzima recuperou 50% de sua atividade inicial aps 10 minutos na presena de Mg2+ em concentraes superiores a 0,1mmol.L-1. Concentraes de 10-4 e 10-3mol.L-1 de Mn2+ e Co2+ foram suficientes para reativar a enzima em 300% comparado ao controle de ons Mn2+ e aproximadamente 100% para ons Co2+. A enzima perdeu gradualmente a sua atividade quando a concentrao foi de 10-2 mol.L-1. Ni2+ e Zn2+ foram incapazes de restabelecer a atividade cataltica. Km app e Vmax app foram 1,95 0,05 mmol.L-1 e 5,40 0,86 x 10-2 mmol.min-1.mg-1. A temperatura e pH timos foram 34C e 7,5. A meia vida da holoenzima foi de 17,5 min a 30C e para a apoenzima foi de 11,0 min a 30C. Quanto variao de pH, a apoenzima provou ser mais sensvel que a holoenzima. Palavras-chave: -galactosidase. ons metlicos divalentes. Atividade enzimtica. Estabilidade.

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Fundao de Amparo Pesquisa do Estado de So Paulo (FAPESP)

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Ps-graduao em Agronomia (Gentica e Melhoramento de Plantas) - FCAV

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Conselho Nacional de Desenvolvimento Cientfico e Tecnolgico (CNPq)

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A detailed theoretical study of the 1,7,1l,17-tetraoxa-2,6,12,16-tetraaza-cycloeicosane ligand ([20]AneN(4)O(4)) coordinated to Fe2+, Co2+, Ni2+, Ru2+, Rh2+, and Pd2+ transition metal ions was carried out with the B3LYP method. Two different cases were performed: when nitrogen is the donor atom (1a (q) ) and also with the oxygen as the donor atom (1b (q) ). For all the cases performed in this study 1a (q) structures were always more stable than the 1b (q) ones. Considering each row is possible to see that the energy increases with the increase of the atomic number. The M2+ cation binding energies for the 1a (q) complexes increase with the following order: Fe2+ &lt; Ru2+ &lt; Co2+ &lt; Ni2+ &lt; Rh2+ &lt; Pd2+.

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This work describes the effects of the cell surface display of a synthetic phytochelatin in the highly metal tolerant bacterium Cupriavidus metallidurans CH34. The EC20sp synthetic phytochelatin gene was fused between the coding sequences of the signal peptide (SS) and of the autotransporter beta-domain of the Neisseria gonorrhoeae IgA protease precursor (IgA beta), which successfully targeted the hybrid protein toward the C. metallidurans outer membrane. The expression of the SS-EC20sp-IgA beta gene fusion was driven by a modified version of the Bacillus subtilis mrgA promoter showing high level basal gene expression that is further enhanced by metal presence in C. metallidurans. The recombinant strain showed increased ability to immobilize Pb2+, Zn2+, Cu2+, Cd2+, Mn2+, and Ni2+ ions from the external medium when compared to the control strain. To ensure plasmid stability and biological containment, the MOB region of the plasmid was replaced by the E. coli hok/sok coding sequence.

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The use of a low-cost benchtop time-domain NMR (TD-NMR) spectrometer to monitor copper electrodeposition in situ is presented. The measurements are based on the strong linear correlation between the concentration of paramagnetic ions and the transverse relaxation rates (R-2) of the solvent protons Two electrochemical NMR (EC-NMR) cells were constructed and applied to monitor the Cu2+ concentration during the electrodeposition reaction. The results show that TD-NMR relaxometry using the Carr-Purcell-Meiboom-Gill pulse sequence can be a very fast, simple, and efficient technique to monitor, in real time, the variation in the Cu2+ concentration during an electrodeposition reaction. This methodology can also be applied to monitor the electrodeposition of other paramagnetic ions, such as Ni2+ and Cr3+, which are commonly used in electroplating.

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An endo-1,5-arabinanase (abnA) encoding gene from Aspergillus niveus was identified, cloned and successfully expressed in Aspergillus nidulans strain A773. Based on amino acid sequence comparison, the 34-kDa enzyme could be assigned to CAZy GH family 43. Characterization of purified recombinant endo-1,5-arabinanase (AbnA) revealed that it is active at a wide pH range (pH 4.0-7.0) and an optimum temperature at 70 degrees C. The immobilization of the AbnA was performed via covalent binding onto agarose-modified supports: glyoxyl iminodiacetic acid-Ni2+, glyoxyl amine, glyoxyl (4% and 10%) and cyanogen bromide activated sepharose. The yield of immobilization was similar on glyoxyl amine and glyoxyl (96%), and higher than glyoxyl iminodiacetic acid-Ni2+ (43%) support. The thermal inactivation of these immobilized preparations showed that the stability of the AbnA immobilized on glyoxyl 4 and 10% was improved by 4.0 and 10.3-fold factor at 70 degrees C. The half-life of glyoxyl 4% derivative at 60 degrees C was &gt;48 h (pH 5), 9 h (pH 7) and 88 min (pH 9). The major hydrolysis product of debranched arabinan or arabinopentaose by glyoxyl agarose-immobilized AbnA was arabinobiose. (C) 2012 Elsevier B.V. All rights reserved.