PubMed · 14074550
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V M CLARK, S G WARREN. 1963-08-17. WHY DO PHOSPHAGENS FUNCTION AS PHOSPHORYL-TRANSFER REAGENTS?. https://doi.org/10.1038/199657a0
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In this work, the effects of fluorination of polyimide thin films on surface and dielectric characteristics were studied using X-ray photoelectron spectroscopy (XPS) and dielectric spectrometry, respectively. The thermal and mechanical properties of the film were characterized by thermogravimetric analysis (TGA) and tensile strengths, respectively. The fluorine content of the polyimide thin film was increased with increasing treatment concentration, resulting in decreasing dielectric constant of the film. It was found that the replacement of fluorine led to the decrease of the local electronic polarizability of polyimide, or to the increase of the free volume, which can be attributed to the relatively large size of fluorine. Nevertheless, the fluorination did not significantly affect thermal or mechanical properties of the polyimide film under mild conditions in this system.
This study demonstrates how chemically interesterified hydrogenated palm oil (IHPO) and partially hydrogenated palm oil (PHPO) can be structured to have similar mechanical properties. Crystallization of IHPO at 30 degrees C for 24 h yielded a fat with a solid fat content (SFC) of 45% and a yield force of 51.5 N. On the other hand, PHPO had a SFC of 50% and a yield force of 44 N when crystallized under the same conditions. The result was opposite from what would be expected from the SFC point of view, thus suggesting that the microstructure of the fat plays a key role in determining mechanical properties. By matching crystallization behavior using the Avrami index as a guide, microstructures and material hardness were successfully matched. These results suggest that the dynamics of structure formation was a key factor influencing the macroscopic mechanical properties of palm oil-based fats.
Changes induced by high pressure (HP) treatment (200-600 MPa) on soybean protein isolates (SPI) at pH 3 (SPI3) and pH 8 (SPI8) were analyzed. Changes in protein solubility, surface hydrophobicity (Ho), and free sulfhydryl content (SH(F)) were determined. Protein aggregation and denaturation and changes in secondary structure were also studied. An increase in protein Ho and aggregation, a reduction of free SH, and a partial unfolding of 7S and 11S fractions were observed in HP-treated SPI8. Changes in secondary structure were also detected, which led to a more disordered structure. HP-treated SPI3 was partially denatured and presented insoluble aggregates. A major molecular unfolding, a decrease of thermal stability, and an increase of protein solubility and Ho were also detected. At 400 and 600 MPa, a decrease of the SH(F) and a total denaturation were observed.