Thermal studies on protein isolates of white lupin seeds (Lupinus albus)

This study used TG, DSC, and SDS-PAGE techniques to study protein isolates (PIs) in the powder form obtained from lupin seeds flour Lupinus albus. Different methods of preparing PIs were tested, resulting in final products that were different only in relation to the yield and protein content. The results of the protein analysis by SDS-PAGE showed that the same protein fractions were present in the lupin seeds and in the obtained PIs. This result shows that the process of extraction was not damaging to the composition of the original protein. On the other hand, the results of the thermal analysis (DSC and TG-DTG curves) obtained for the different PIs, led to the detection of changes in the protein conformation through the Delta H values, which in general decreased with increasing values of pH and ionic strength in the experimental conditions of extraction.Predilecta Foods (Sao Lourenco do Turvo, SP, Brazil)CAPES Foundation (Brazil

Thermal study of the solid-state reactions on Pt-15%Rh/Hg system

Thermogravimetry (TG), energy dispersive X-ray microanalysis (EDX), scanning electron microscopy (SEM), mapping surface and X-ray diffraction (XRD) were used for the study of solid-state reaction on Pt-15%Rh with electrodeposited mercury. The results suggest when heated the mercury film react with the Pt-15%Rh alloy to form intermetallics having different thermal stabilities indicated by three mass loss steps. The first mass loss step occurs between room temperature and 184 degrees C only the bulk Hg is removed and PtHg4, PtHg2 and RhHg2 were characterized by XRD. The second step, between 184 and 271 degrees C, was attributed to PtHg4 decomposition with formation of PtHg2 stabilized by RhHg2. The third step, between 271 and 340 degrees C, was attributed to decomposition of a solid-solution of PtHg2/RhHg2. The fourth step, between 340 and 600 degrees C, was ascribed to: (1) a thermal decomposition of PtHg2, formed by a PtHg eutectoid reaction (similar to 340 degrees C) on the surface and (2) Hg removal from a solid solution of Pt-15%Rh(Hg). (C) 2013 Elsevier B.V. All rights reserved

Isolado protéico de semente de goiaba (Psidium guajava): caracterização de propriedades funcionais Protein isolate of guava seed (Psidium guajava): functional properties of characterization

Isolados protéicos (IPs) foram obtidos a partir da farinha da semente de goiaba (Psidium guajava) por extração a diferentes pHs seguido de precipitação isoelétrica (pI 4,5). As condições para o preparo do IP foram definidas a partir da curva de solubilidade, em pH 10,0 e 11,5, na ausência de NaCl e em temperatura de 25 ± 3 ºC. Essas condições levaram a um rendimento na extração de 45,19 e 66,23%, e teor protéico de 96,4 e 93,5% para IP 10,0 e 11,5, respectivamente. Capacidade de absorção de água e óleo de 1,05 ± 0,07 e 2,30 ± 0,01 mL.g-1 proteína e 1,65 ± 0,07 e 1,70 ± 0,07 mL.g-1 proteína foram obtidos, respectivamente, para IP 10,0 e IP 11,5. Não foram observadas diferenças entre os IPs quanto à atividade e estabilidade de emulsão, atingindo valores similares e superiores ao IP de outras sementes. Formação de gel, em pH neutro e ausência de sal, exigiram concentrações de 8 e 10% para IP 10,0 e IP 11,5, respectivamente. Maior capacidade de formação de espuma foi obtida para IP 10,0 em pH neutro e alcalino, apresentando valores de até 90% do volume inicial, por outro lado, para estabilidade de espuma, ambos IPs apresentaram boas propriedades até duas horas após a formação da espuma.<br>Protein isolates (PIs) were obtained from the guava seed flour (Psidium guajava) by extracting different pHs followed by isoelectric precipitation (pH 4.5). The conditions for preparation of the PIs were defined from the solubility curve at pH 10.0 and 11.5, in the absence of NaCl and a temperature of 25 ± 3 ºC. These conditions obtained protein isolated (PI) with extraction yield of 45.19 and 66.23%, with protein content of 96.4 and 93.5% for PI 10.0 and 11.5, respectively. The water and oil absorption capacity of 1.05 ± 0.07 and 2.30 ± 0.01 mL.g-1 protein and 1.65 ± 0.07 and 1.70 ± 0.07 mL.g-1 protein, respectively; were obtained for PI 10.0 and PI 11.5. Differences among the PIs regarding the emulsion activity and stability were not observed, reaching similar and higher values compared to IP of other seeds. The gel formation in neutral pH and salt absence require concentrations of 8 and 10% to PI 10.0 and PI 11.5, respectively. The highest foam formation was observed for PI 10.0 in neutral and alkaline pH, and it showed a capacity of up to 90% of the initial volume; however for the foam stability both IPs showed good properties of up to two hours after foam formation

A Solid Film Electrode of Intermetallic Ag 2 Hg 3.02 for the Direct Determination of Folic Acid in Fresh and Processed Fruit Juices

AgSIE was used for the direct analysis of folic acid (FA), with a detection limit and lower level of quantitation of 6.8 x10-10 mol L-1 and 2.3 x 10 8 mol L-1. The analysis in fresh and processed fruits was done without any sample pretreatment. In strawberry and acerola juices, FA concentration level values were below the method detection limit. FA was detectable in peach (77.7 0.4 mg L-1 and 64.4 0.5 mgL-1), Persian lime (45.4 0.7 mg L-1), pineapple Hawaii (66.2 0.4 mgL-1), pear pineapple (35.3 0.6 mgL-1), cashew (54.4 0.5 mgL-1) , passion fruit (73.2 0.3 mgL-1), and apple (84.4 0.5 mg L-1 )