Nickel-Alumina Catalysts for the Transformation of Vegetable Oils into Green Diesel: The Role of Preparation Method, Activation Temperature, and Reaction Conditions.

Two nickel alumina catalysts containing 60 wt. % Ni were synthesized by wet impregnation and co-precipitation in order to study the effect of preparation methods on the catalytic efficiency concerning the transformation of sunflower oil into green diesel. The effect of activation temperature on the catalytic efficiency of the most active catalyst was also studied. The catalysts were characterized using various techniques and which were evaluated in the aforementioned reaction using a semi-batch reactor. The catalyst prepared by co-precipitation exhibited a higher specific surface area and smaller mean crystal size of the nickel nanoparticle (higher nickel metallic surface). These justify its higher efficiency with respect to the corresponding catalyst synthesized by wet impregnation. The increase in the activation temperature from 400 to 600 °C increased the size of the nickel nanoparticles through sintering, thus destroying the small pores. These led to a decrease in the nickel surface and specific surface area and, thus, to a decrease in the catalytic efficiency. The optimization of the reaction conditions over the most active catalyst (prepared by co-precipitation and activated at 400 °C) leads to the complete transformation not only of the sunflower oil (edible oil) but also of waste cooking oil (non-edible oil) into green diesel. The liquid produced after the hydrotreatment for these two feedstocks for 7 h, at H2 pressure 40 bar and temperature 350 °C using 100 mL of oil and 1 g of catalyst was composed of 97 and 96 wt. % of green diesel, respectively.

Liposomal Entrapment or Chemical Modification of Relaxin2 for Prolongation of Its Stability and Biological Activity.

Relaxin (RLX) is a protein that is structurally similar to insulin and has interesting biological activities. As with all proteins, preservation of RLX's structural integrity/biological functionality is problematic. Herein, we investigated two methods for increasing the duration of relaxin-2's (RLX2) biological activity: synthesis of a palmitoyl RLX2 conjugate (P-RLX2) with the use of a Palmitoyl-l-Glu-OtBu peptide modifier, and encapsulation into liposomes of P-RLX2, RLX2, and its oxidized form (O-RLX2). For liposomal encapsulation thin-film hydration and DRV methods were applied, and different lipid compositions were tested for optimized protein loading. RLX2 and O-RLX2 were quantified by HPLC. The capability of the peptides/conjugate to stimulate transfected cells to produce cyclic adenosine monophosphate (cAMP) was used as a measure of their biological activity. The stability and bioactivity of free and liposomal RLX2 types were monitored for a 30 d period, in buffer (in some cases) and bovine serum (80%) at 37 °C. The results showed that liposome encapsulation substantially increased the RLX2 integrity in buffer; PEGylated liposomes demonstrated a higher protection. Liposome encapsulation also increased the stability of RLX2 and O-RLX2 in serum. Considering the peptide's biological activity, cAMP production of RLX2 was higher than that of the oxidized form and the P-RLX2 conjugate (which demonstrated a similar activity to O-RLX2 when measured in buffer, but lower when measured in the presence of serum proteins), while liposome encapsulation resulted in a slight decrease of bioactivity initially, but prolonged the peptide bioactivity during incubation in serum. It was concluded that liposome encapsulation of RLX2 and synthetic modification to P-RLX2 can both prolong RLX2 peptide in vitro stability; however, the applied chemical conjugation results in a significant loss of bioactivity (cAMP production), whereas the effect of liposome entrapment on RLX2 activity was significantly lower.