Quark Matter in a Strong Magnetic Background

In this chapter, we discuss several aspects of the theory of strong interactions in presence of a strong magnetic background. In particular, we summarize our results on the effect of the magnetic background on chiral symmetry restoration and deconfinement at finite temperature. Moreover, we compute the magnetic susceptibility of the chiral condensate and the quark polarization at zero temperature. Our theoretical framework is given by chiral models: the Nambu-Jona-Lasinio (NJL), the Polyakov improved NJL (or PNJL) and the Quark-Meson (QM) models. We also compare our results with the ones obtained by other groups.Comment: 34 pages, survey. To appear in Lect. Notes Phys. "Strongly interacting matter in magnetic fields" (Springer), edited by D. Kharzeev, K. Landsteiner, A. Schmitt, H.-U. Ye

Reatividade in vitro de lipase submetida a diferentes tratamentos tecnológicos Reactivity in vitro of the lipase submitted to different technological treatments

Analisou-se a atividade enzimática in vitro de uma lipase em diferentes condições de temperatura (simulando o processo de peletização) e pH (acidez gástrica) e na presença de íons minerais e metálicos. Para avaliar a estabilidade térmica, a enzima foi incubada a 80(0)C por quatro tempos (0, 5, 10 e 15 minutos). O efeito do pH foi estudado submetendo-se a enzima a quatro valores de pH (7,3, 2,0, 3,2 e 5,0). Para avaliar o efeito da lipase na presença de íons minerais e metálicos, incubou-se a enzima em diferentes soluções contendo cálcio, cobre, cobalto, manganês e ferro. Frente às diferentes condições, a lipase conservou atividade parcial, mas não pôde ser considerada uma enzima ideal em função do efeito inibidor promovido pelo pH ácido e pelas soluções iônicas testadas.<br>The in vitro catalytic activity of a lipase was assessed in different conditions of temperature (simulating that of pelleted ration manufacturing), pH (gastric acidity), and its stability in the presence of metallic and mineral ions. To assess the thermal stability, the enzyme was incubated for 0, 5, 10 or 15 minutes at 80ºC. The effect of pH was studied by submitting the lipase to pH values of 7.3, 2.0, 3.2 or 5.0. In order to evaluate the catalytic activity in the presence of metallic and mineral ions, the enzyme was incubated in solutions containing calcium, copper, cobalt, manganese and iron. In the above mentioned conditions, the lipase partially preserved its activity, but, could not be considered an ideal enzyme due to its inhibition by the acidic pH and the ionic solutions tested