Uso do poli (tereftalato de etileno) no pós-tratamento de água para a remoção de fármacos residuais

Pós-graduação em Engenharia Civil - FEIS

Avaliação do desenvolvimento e a eficiência do capim vetiver (chrysopogon zizanioides) em sistemas híbridos de alagados construídos

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Purification and structural characterization of snake venom proteins

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Avaliação do potencial de reuso agrícola do efluente de uma estação de tratamento de esgoto com alagados construídos

Pós-graduação em Agronomia (Energia na Agricultura) - FCA

Induction of suppressiveness to Fusarium wilt of chrysanthemum with composted sewage sludge

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Rapid purification of serine proteinases from Bothrops alternatus and Bothrops moojeni venoms

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

PURIFICATION AND CHARACTERIZATION OF SOY COTYLEDON -GLUCOSIDASE

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Purification and biochemical characterization of an alkaline pectin lyase from Fusarium decemcellulare MTCC 2079 suitable for Crotolaria juncea fiber retting

An extracellular pectin lyase secreted by Fusarium decemcellulare MTCC 2079 under solid state fermentation condition has been purified to electrophoretic homogeniety by using ammonium sulfate fractionation, carboxymethyl cellulose and gel filtration (Sephadex G-100) column chromatographies. The purified enzyme showed single protein band corresponding to molecular mass 45 +/- 01 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had maximum activity at pH 9.0 and showed maximum stability in the pH range of 9.0-12.0. The optimum temperature of the purified enzyme was 50 degrees C and it showed maximum stability upto 40 degrees C. The energy of activation for the thermal denaturation (Ea) was 59.06 kJ mol(-1) K-1. The K-m and k(cat) values using citrus pectin as the substrate were 0.125mgml(-1) and 72.9 s(-1) in 100mM sodium carbonate buffer pH 9.0 at 50 degrees C. The biophysical studies on pectin lyase showed that its secondary structure belongs to alpha+beta class of protein with comparatively less of beta-sheets. Purified pectin lyase showed efficient retting of Crotolaria juncea fibers.

Precificação do biogás produzido por autoprodutores, considerando seu transporte por meio de gasodutos existentes

The expansion of the energy matrix is a matter of great importance since the recent problems facing the country in this sector, such as rationing mobilized in 2001. Moreover, there is also concern with global sustainable development. Brazil is producing about 64 million cubic meters of biogas per day, but only a small percentage of this total is harnessed as an energy resource. Compounders are considered potential, for example, landfill energy (LE) and sewage treatment plants (STP), which can be adapted to produce biogas and market them. The work focuses its studies on biogas produced by these small and medium compounders. Are proposed and studied the following alternatives for the utilization of biogas energy: generation and sale of electricity through the installation of a small power station within the landfill, and purification and marketing of gas, whose price will be a consideration on the price of natural gas, taking into account the percentage of methane present in the biogas. Trade ensures that gas plus a destination ecologically appropriate to it, taking advantage of its energy

Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation

Polygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used in food industries, textile processing, degumming of plant rough fibres, and treatment of pectic wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was carried out in culture media containing sugar cane bagasse and orange bagasse in proportions of 30% and 70% (w/w) at 45°C for 4 days. PG obtained was purified by gel filtration and ion-exchange chromatography. The highest activity was found between pH 4.5 and 5.5, and the enzyme preserved more than 80% of its activity at pH values between 5.0 and 6.5. At pH values between 3.0 and 4.5, PG retained about 73% of the original activity, whereas at pH 10.0 it remained around 44%. The optimum temperature was 60–65°C. The enzyme was completely stable when incubated for 1 hour at 50°C. At 55°C and 60°C, the activity decreased 55% and 90%, respectively. The apparent molecular weight was 29.3 kDa, Km of 1.58 mg/mL and Vmax of 1553.1μmol/min/mg. The presence of Zn+2, Mn+2, and Hg+2 inhibited 59%, 77%, and 100% of enzyme activity, respectively. The hydrolysis product suggests that polygalacturonase was shown to be an endo/exoenzyme.

Partial purification, immobilization and preliminary biochemical characterization of lipases from Rhizomucor pusillus

Lipases have important applications in biotechnological processes, motivating us to produce, purify, immobilize and perform a biochemical characterization of the lipase from Rhizomucor pusillus. The fungus was cultivated by solid state fermentation producing lipolytic activity of about 0.5 U/mL(4U/g). A partial purification by gel filtration chromatography in Se-phacryl S-100 allowed obtaining a yield of about 85% and a purification factor of 5.7. Our results revealed that the purified enzyme is very stable with some significant differences in its properties when compared to crude extract. The crude enzyme extract has an optimum pH and temperature of 7.5 ° C and 40 ° C, respectively. After purification, a shift of the optimum pH from 7 to 8 was observed, as well as a rise in optimumtemperature to 60 ° C and an increase in stability. The enzyme was immobilized on CNBr-Agarose and Octyl-Agarose supports, having the highest immobilization yield of 94% in the second resin. The major advantage of immobilization in hydrophobic media such as Octyl is in its hyper activation, which in this case was over 200%, a very interesting finding. Another advantage of this type of immobilization is the possibility of using the derivatives in biotechnological applications, such as in oil enriched with omega-3 as the results obtained in this study display the hydrolysis of 40% EPA and 7% DHA from sardine oil, promising results compared to the literature.

Expression, purification and characterization of cold shock protein A of Corynebacterium pseudotuberculosis

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Magnetic Purification of Curcumin from Curcuma longa Rhizome by Novel Naked Maghemite Nanoparticles

Naked maghemite nanoparticles, namely, surface active maghemite nanoparticles (SAMNs), characterized by a diameter of about 10 nm, possessing peculiar colloidal stability, surface chemistry, and superparamagnetism, present fundamental requisites for the development of effective magnetic purification processes for biomolecules in complex matrices. Polyphenolic molecules presenting functionalities with different proclivities toward iron chelation were studied as probes for testing SAMN suitability for magnetic purification. Thus, the binding efficiency and reversibility on SAMNs of phenolic compounds of interest in the pharmaceutical and food industries, namely, catechin, tyrosine, hydroxytyrosine, ferulic acid, coumaric acid, rosmarinic acid, naringenin, curcumin, and cyanidin-3-glucoside, were evaluated. Curcumin emerged as an elective compound, suitable for magnetic purification by SAMNs from complex matrices. A combination of curcumin, demethoxycurcumin, and bis-demethoxycurcumin was recovered by a single magnetic purification step from extracts of Curcuma longa rhizomes, with a purity >98% and a purification yield of 45%, curcumin being >80% of the total purified curcuminoids.

Polyphenol oxidase from sweet potato: Purification and properties

Polyphenol oxidase (PPO, EC 1.14.18.1) extracted from sweet potato root [Ipomoea batatas (L.) Lam.] was purified 189-fold by precipitation with ammonium sulfate and elution from columns of Sephadex G-25, DEAE-cellulose, and Sephadex G-100. Polyacrylamide gel electrophoresis of the purified preparation revealed that PPO was highly purified by the procedure adopted. The purified enzyme had an estimated molecular weight of 96 000 and Km values of 26, 8, 5, and 96 mM for 4-methylcatechol, chlorogenic acid, caffeic acid, and catechol, respectively. The optimum pH varies from about 4.0 to 6.5, depending on the substrate. PPO activity was inhibited by p-coumaric and cinnamic acids, sodium metabisulfite, dithioerythritol, ascorbic acid, L-lysine, D-phenylalanine, L-methionine, glycine, L-isoleucine, and L-glutamine. Heat inactivation between 60 and 80 °C was biphasic. Sucrose, (NH4)2SO4, NaCl, and KCl appeared to be protective agents of sweet potato PPO against thermal denaturation. © 1992 American Chemical Society.