Excess Enthalpies Analysis of Biofuel Components: Sunflower Oil-Alcohols Systems.

This study addresses the pressing issues of energy production and consumption, in line with global sustainable development goals. Focusing on the potential of alcohols as "green" alternatives to traditional fossil fuels, especially in biofuel applications, we investigate the thermochemical properties of three alcohols (n-propanol, n-butanol, n-pentanol) blended with sunflower oil. The calorimetric analysis allows for the experimental determination of excess enthalpies in pseudo-binary mixtures at 303.15 K, revealing similarities in the trends of the curves (dependence on concentrations) but with different values for the excess enthalpies for each mixture. Despite the structural differences of the alcohols studied, the molar excess enthalpy values exhibit uniformity, suggesting consistent mixing behavior. The peak values of excess enthalpies for systems with sunflower oil and n-propanol, n-butanol and n-pentanol are, respectively, 3255.2 J/mole, 3297.4 J/mole and 3150.1 J/mole. Both the NRTL and Redlich-Kister equations show satisfactory agreement with the obtained values.

Excess Enthalpies for Binary Mixtures of the Reactive System Acetic Acid + n-Butanol + n-Butyl Acetate + Water: Brief Data Review and Results at 313.15 K and Atmospheric Pressure.

The data on molar excess enthalpies, HmE, for the binary mixtures acetic acid + n-butanol, acetic acid + n-butyl acetate and n-butanol + n-butyl acetate at 313.15 K and atmospheric pressure were obtained with use of the C80 isothermal mixing calorimeter (Setaram). The correlation of the data was carried out using the NRTL model and Redlich-Kister equation. A comparative analysis with the literature data on all available binary subsystems of the quaternary system was carried out. Other thermodynamic properties (Cp,mE, SmE, ΔmixSm, GmE and ΔmixGm) of the binary systems were estimated using literature data and well-known formulas of classical thermodynamics.

Impact of Layered Perovskite Oxide La0.85Yb0.15AlO3 on Structure and Transport Properties of Polyetherimide.

This study aims to improve properties of Ultem® polyetherimide (PEI) by incorporating up to 2 wt% additives of the perovskite oxide La0.85Yb0.15AlO3 (LYA). The structure of dense PEI/LYA films was characterized by X-ray diffraction (XRD) and scanning electron microscopy (SEM) in combination with an analysis of their elemental composition using energy-dispersive spectroscopy (EDS). The PEI/LYA films exhibit a two-layer structure. Contact angle measurements revealed hydrophilization of the membrane surface enriched with the perovskite. The transport properties were tested via gas separation and pervaporation processes. The separation selectivity of He/N2 and O2/N2 gas pairs increased with the growth of the LYA content in the membranes. Pervaporation of a methanol(MeOH)-cyclohexane(CH) mixture was effective due to the high sorption of MeOH in the PEI/LYA membranes. The maximal pervaporation separation index was found for the PEI/LYA(2%) membrane.

Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein.

The ability of d-glucose/d-galactose-binding protein (GGBP) to reversibly interact with its ligands, glucose and galactose, makes this protein an attractive candidate for sensing elements of glucose biosensors. This potential is largely responsible for attracting researchers to study the conformational properties of this protein. Previously, we showed that an increase in the fluorescence intensity of the fluorescent dye 6-bromoacetyl-2-dimetylaminonaphtalene (BADAN) is linked to the holo-form of the GGBP/H152C mutant in solutions containing sub-denaturing concentrations of guanidine hydrochloride (GdnHCl). It was hypothesized that low GdnHCl concentrations might lead to compaction of the protein, thereby facilitating ligand binding. In this work, we utilize BADAN fluorescence spectroscopy, intrinsic protein UV fluorescence spectroscopy, and isothermal titration calorimetry (ITC) to show that the sub-denaturing GdnHCl concentrations possess osmolyte-like stabilizing effects on the structural dynamics, conformational stability, and functional activity of GGBP/H152C and the wild type of this protein (wtGGBP). Our data are consistent with the model where low GdnHCl concentrations promote a shift in the dynamic distribution of the protein molecules toward a conformational ensemble enriched in molecules with a tighter structure and a more closed conformation. This promotes the increase in the configurational complementarity between the protein and glucose molecules that leads to the increase in glucose affinity in both GGBP/H152C and wtGGBP.