Hydrothermal synthesis of a photocatalyst based on Byrsonima crassifolia and TiO2 for degradation of crystal violet by UV and visible radiation.

This work presents a one-step synthesis methodology for preparing a hydrochar (HC) doped with TiO2 (HC-TiO2) for its application on the degradation of crystal violet (CV) using UV and visible radiation. Byrsonima crassifolia stones were used as precursors along with TiO2 particles. The HC-TiO2 sample was synthesized at 210 °C for 9 h using autogenous pressure. The photocatalyst was characterized to evaluate the TiO2 dispersion, specific surface area, graphitization degree, and band-gap value. Finally, the degradation of CV was investigated by varying the operating conditions of the system, the reuse of the catalyst, and the degradation mechanism. The physicochemical characterization of the HC-TiO2 composite showed good dispersion of TiO2 in the carbonaceous particle. The presence of TiO2 on the hydrochar surface yields a bandgap value of 1.17 eV, enhancing photocatalyst activation with visible radiation. The degradation results evidenced a synergistic effect with both types of radiation due to the hybridized π electrons in the sp2-hybridized structures in the HC surface. The degradation percentages were on average 20% higher using UV radiation than visible radiation under the following conditions: [CV] = 20 mg/L, 1 g/L of photocatalyst load, and pH = 7.0. The reusability experiments demonstrated the feasibility of reusing the HC-TiO2 material up to 5 times with a similar photodegradation percentage. Finally, the results indicated that the HC-TiO2 composite could be considered an efficient material for the photocatalytic treatment of water contaminated with CV.

Application of Raman spectroscopy for the determination of proteins denaturation and amino acids decomposition temperature.

Raman spectroscopy was employed to study the thermal denaturation of three different proteins, bovine serum albumin (BSA), lysozyme, ovalbumin; and the decomposition temperature of three amino acids, l-glutamine, l-cysteine, and l-alanine, all of them as lyophilized powders. All the Raman bands observed in the spectra obtained were recorded and analyzed at preset heating temperatures. The results obtained for either protein denaturation temperature TD and amino acid decomposition temperatures TM-dc, were compared with those measured by differential scanning calorimetry (DSC). The DSC and Raman results were additionally corroborated with a thermogravimetric analysis (TGA) for the case of proteins. This exercise indicated almost complete coincidence in the determination of these transition temperatures between the three techniques, evidencing the applicability of Raman spectroscopy in the study of denaturation and decomposition temperatures of proteins and amino acids.

Determination of the denaturation temperature of the Spike protein S1 of SARS-CoV-2 (2019 nCoV) by Raman spectroscopy.

In the present work the temperature response of the constitutive S1 segment of the SARS-CoV-2 Spike Glycoprotein (GPS) has been studied. The intensity of the Raman bands remained almost constant before reaching a temperature of 133 °C. At this temperature a significant reduction of peak intensities was observed. Above 144 °C the spectra ceased to show any recognizable feature as that of the GPS S1, indicating that it had transformed after the denaturation process that it was subjected. The GPS S1 change is irreversible. Hence, Raman Spectroscopy (RS) provides a precision method to determine the denaturation temperature (TD) of dry powder GPS S1. The ability of RS was calibrated through the reproduction of TD of other well studied proteins as well as those of the decomposition temperature of some amino acids (AA). Through this study we established a TD of 139 ± 3 °C for powder GPS S1 of SARS-CoV-2.