Synergistic effect in the catalytic activity of lipase Rhizomucor miehei immobilized on zeolites for the production of biodiesel

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

Allosteric water and phosphate effects in Hoplosternum littorale hemoglobins

This paper reports the results obtained using the osmotic stress method applied to the purified cathodic and anodic hemoglobins (Hbs) from the catfish Hoplosternum littorale, a species that displays facultative accessorial air oxygenation. We demonstrate that water potential affects the oxygen affinity of H. littorale Hbs in the presence of an inert solute (sucrose). Oxygen affinity increases when water activity increases, indicating that water molecules stabilize the high-affinity state of the Hb. This effect is the same as that observed in tetrameric vertebrate Hbs. We show that both anodic and cathodic Hbs show conformational substrates similar to other vertebrate Hbs. For both Hbs, addition of anionic effectors, especially chloride, strongly increases the number of water molecules bound, although anodic Hb did not exhibit sensitivity to saturating levels of ATP. Accordingly, for both Hbs, we propose that the deoxy conformations coexist in at least two anion-dependent allosteric states, T-o and T-x, as occurs for human Hb. We found a single phosphate binding site for the cathodic Hb.

Influência da temperatura e da concentração do cloreto de sódio (NaCl) nas isotermas de sorção da carne de tambaqui (Colossoma macroparum)

As isotermas de sorção da carne de tambaqui desidratada osmoticamente foram determinadas a três temperaturas (5, 17 e 29ºC) e com duas concentrações de solução osmótica (10 e 30% de NaCl), pelo método gravimétrico. Quatro modelos de sorção foram testados para verificar o melhor ajuste; GAB, Oswin, BET e PELEG. Os dados experimentais se ajustaram satisfatoriamente aos modelos. O modelo escolhido para este trabalho foi o de PELEG. Para o ajuste nas curvas de sorção, foi feita a análise de regressão não-linear, usada o programa estatístico ORIGIN 4.0 para estimar as constantes dos modelos. A avaliação do melhor ajuste foi feita pela análise do coeficiente de determinação do ajuste (r²) e teste de Qui-quadrado (x²). Foram analisadas as influências da variação da temperatura e concentração de NaCl na atividade de água da carne do tambaqui. À medida que decresce a temperatura há um decréscimo na atividade de água. Um aumento na concentração do NaCl diminui a atividade de água. A propriedade termodinâmica estudada foi o calor isostérico de sorção. A medida que aumenta a concentração da solução osmótica aumenta o valor do calor isostérico de sorção.

INFLUENCE of ENCAPSULATING MATERIALS on WATER SORPTION ISOTHERMS of VACUUM-DRIED PERSIMMON PULP POWDER

Water sorption isotherms for vacuum-dried persimmon pulp (PP) powder were determined in the temperature range of 20-50C, and the effects of maltodextrin (MD) or gum arabic (GA) addition on the water sorption behavior of the dried powders were analyzed. Several models were evaluated to fit the experimental data and the Guggenheim-Anderson-de Boer model was selected as the most adequate to describe the observed behavior. Addition of encapsulants affected the isotherms: at the same water activity, PP powder with added GA (PP + GA) or MD (PP + MD) presented lower equilibrium water content than pure PP and were less affected by temperature variations. Samples of PP + MD presented lower equilibrium moisture content than those of PP + GA. The isosteric heats of sorption of pulp powders with encapsulants were higher (less negative) than those of PP, suggesting that there are more active polar sites in PP than in pulp powder containing encapsulants.PRACTICAL APPLICATIONSThe choice of persimmon to carry out this work was due to the large persimmon production available in Brazil; moreover, persimmon pulp is rich in vitamin C, vitamin A and iron, as well as in phenolic compounds. Drying of fruit pulps with high sugar content presents technical difficulties because the hygroscopicity and thermoplasticity of the resulting powders when exposed to high temperature and relative humidity. For this reason, addition of high-molar-mass biopolymers, such as maltodextrin or gum arabic, is a strategy to aid drying and to improve storage stability. Knowledge of water sorption isotherms and net isosteric heats of sorption is important to various food processing operations, including drying, storage and packaging. They are useful in calculating time and energy consumptions during drying, modeling moisture changes during storage and predicting shelf life of food products.

Thermodynamic properties of water sorption of jackfruit (Artocarpus heterophyllus Lam.) as a function of moisture content

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Study of the enthalpy-entropy mechanism from water sorption of orange seeds (C. sinensis cv. Brazilian) for the use of agro-industrial residues as a possible source of vegetable oil production

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

Effect of maltodextrin and arabic gum in water vapor sorption thermodynamic properties of vacuum dried pineapple pulp powder

Moisture equilibrium data of pineapple pulp (PP) powders with and without additives - 18% maltodextrin (MD) or 18% gum Arabic (GA) - were determined at 20, 30, 40 and 50 degrees C by using the static gravimetric method in a water activity range of 0.06-0.90. The obtained isotherms were sigmoid, typical type 111, and the Guggenhein-Anderson-de Boer (GAB) model was fitted to the experimental data of equilibrium moisture content versus water activity. Addition of additives was shown to affect the isotherms in such a way that, at the same water activity, samples PP + GA and PP + MD presented lower equilibrium moisture content and were not so affected by varying temperature. The net isosteric heats of sorption of pulp powders with additives were higher (less negative) than those of pineapple pulp powders, suggesting that there are more active polar sites in the product without addition of GA or MD. An empirical exponential relationship could describe the heat of sorption dependence on the material moisture content. (C) 2007 Elsevier Ltd. All rights reserved.

The role of hydration on the mechanism of allosteric regulation: In situ measurements of the oxygen-linked kinetics of water binding to hemoglobin

We report here the first direct measurements of changes in protein hydration triggered by a functional binding. This task is achieved by weighing hemoglobin (Hb) and myoglobin films exposed to an atmosphere of 98%, relative humidity during oxygenation. The binding of the first oxygen molecules to Hb tetramer triggers a change in protein conformation, which increases binding affinity to the remaining empty sites giving rise to the appearance of cooperative phenomena. Although crystallographic data have evidenced that this structural change increases the protein water-accessible surface area, isobaric osmotic stress experiments in aqueous cosolutions have shown that water binding is linked to Hb oxygenation. Now we show that the differential hydration between fully oxygenated and fully deoxygenated states of these proteins, determined by weighing protein films with a quartz crystal microbalance, agree with the ones determined by osmotic stress in aqueous cosolutions, from the linkage between protein oxygen affinity and water activity. The agreements prove that the changes in water activity brought about by adding osmolytes to the buffer solution shift biochemical equilibrium in proportion to the number of water molecules associated with the reaction. The concomitant kinetics of oxygen and of water binding to Hb have been also determined. The data show that the binding of water molecules to the extra protein surface exposed on the transition from the low-affinity T to the high-affinity R conformations of hemoglobin is the rate-limiting step of Hb cooperative reaction. This evidences that water binding is a crucial step on the allosteric mechanism regulating cooperative interactions, and suggests the possibility that environmental water activity might be engaged in the kinetic control of some important reactions in vivo.

Water regulation of actinomycin-D binding to DNA: the interplay among drug affinity, DNA long-range conformation, and hydration

Actiaomycin-D (actD) binds to natural DNA at two different classes of binding sites, weak and strong. The affinity for these sites is highly dependent on DNA se(sequence and solution conditions, and the interaction appears to be purely entropic driven Although the entropic character of this reaction has been attributed to the release of water molecules upon drug to DNA complex formation, the mechanism by which hydration regulates actD binding and discrimination between different classes of binding sites on natural DNA is still unknown. In this work, we investigate the role of hydration on this reaction using the osmotic stress method. We skew that the decrease of solution water activity, due to the addition of sucrose, glycerol ethylene glycol, and betaine, favors drug binding to the strong binding sites on DNA by increasing both the apparent binding affinity Delta G, and the number of DNA base pairs apparently occupied by the bound drug n(bp/actD). These binding parameters vary linearly with the logarithm of the molar fraction of water in solution log(X-w), which indicates the contribution of water binding to the energetic of the reaction. It is demonstrated that the hydration change measured upon binding increases proportionally to the apparent size of the binding site n(bp/uctD). This indicates that n(bp/actD) measured from the Scatchard plod is a measure of the size of the DNA molecule changing conformation due to ligand binding. We also find that the contribution of DNA deformation, gauged by n(bp/act) to the total free energy of binding Delta G, is given by Delta G = Delta G(local) + n(bp/actD) x delta G(DNA), where Delta G(local), = -8020 +/- 51 cal/mol of actD bound and delta G(DNa) = -24.1 +/- 1.7cal/mol of base pair at 25 degrees C. We interpret Delta G(local), as the energetic contribution due to the direct interactions of actD with the actual tetranucleotide binding site, and it n(bp/actB) X delta G(DNA) as that due to change inconformation, induced by binding, of it n(bp/actD) DNA base pairs flanking the local site. This interpretation is supported by the agreement found between the value of delta G(DNA) and the torsional free energy change measured independently. We conclude suggesting an allosteric model for ligand binding to DNA, such that the increase in binding affinity is achieved by increasing the relaxation of the unfavorable free energy of binding storage at the local site through a larger number of DNA base pairs. The new aspect on this model is that the size of the complex is not fixed but determined by solutions conditions, such as water activity, which modulate the energetic barrier to change helix conformation. These results may suggest that long-range allosteric transitions of duplex DNA are involved in the inhibition of RNA synthesis by actD, and more generally, in the regulation of transcription. (C) 2000 John Wiley & Sons, Inc.

Óleos essenciais: verificação da ação antimicrobiana in vitro, na água e sobre a microbiota da pele humana

Pós-graduação em Biologia Geral e Aplicada - IBB

Avaliação da desidratação de mamão utilizando métodos combinados

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Effect of calcium on the osmotic dehydration kinetics and quality of pineapple

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Study of thermodynamic water properties and moisture sorption hysteresis of mango skin

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Influence of alternative drying aids on water sorption of spray dried mango mix powders: a thermodynamic approach

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