Enzymatic and Synthetic Routes of Castor Oil Epoxidation

Epoxidation of castor oil in synthetic and enzymatic routes was carried out in order to promote a system with less environmental impact. The epoxidation reactions of castor oil compounds upon addition of lipase enzyme with and without acrylic immobilization and with reaction times of 24 and 6 h, as well as the synthetic compounds upon addition of Amberlite resin and formic acid, were investigated using Fourier transform infrared spectroscopy (FTIR) and nuclear magnetic resonance in hydrogen molecules ((1)H-NMR). The analysis indicated that the enzymatic reactions (6 h) and synthetic reactions provided a conversion from 50 to 96% and epoxidation from 25 to 48%, resulting from peak stretching and signal disintegration in the hydroxyl region due to the appearance of H(2)O in the interaction of peracid with catalyst. In systems without toluene, a dehydration event with a peak absorbance of 0.02 AU, indicating a possible vinyl group at 2355 cm(−1) in enzymatic reactions without acrylic immobilization, was observed and resulted in a selectivity of 2%. In the absence of a solid catalyst, an unsaturation conversion of castor oil above 90% was achieved; however, this catalyst is necessary for the epoxidation to take place, whereas the lipase enzyme becomes able of epoxidizing and dehydrating the castor oil upon changing the time or reaction system. The conversation from 28 to 48% of solid catalysts (Amberlite and lipase enzyme) displays their importance to the instauration conversion of castor oil into oxirane rings.