Mechanism and Kinetics of Lipase-Catalyzed Polycondensation of Glycerol and Sebacic Acid: Influence of Solvent and Temperature.

The mechanism for the Candida antactica lipase B (CALB)-catalyzed polycondensation of glycerol and sebacic acid in polar solvents was proposed based on the profile of formation and consumption of the glyceridic species in the reaction media and on the occurrence of the acyl migration reaction. The acyl migration is mainly responsible for the esterification of the secondary hydroxyl of glycerol and in an opposite way to the regioselective CALB-catalyzed esterification of primary hydroxyls. The enzymatic esterification of glycerol primary hydroxyls occurs preferentially up to carboxylic acid conversions of approximately 0.60-0.75 with rate constants in the range of 0.07-1.44 L mol -1 h -1 , depending on the solvent. Above carboxylic acid conversions of 0.60-0.75, acyl migration occurs in parallel to enzymatic esterification with rate constants of approximately 0.04-0.12 h -1 and is the rate-limiting step of the polymerization. The hydrogen bonding accepting ability of the solvents is the main parameter that dictates the enzymatic catalysis rate. However, the magnitude of the polymer-solvent interaction governs the polymer chain growth. Acetonitrile has a lower hydrogen bonding accepting ability and a less favorable polymer-solvent interaction compared with the other polymer-solvent pairs, and polycondensation achieves the highest enzymatic rate constant of approximately 0.84-1.44 L mol -1 h -1 ; however, low molar mass polymers with M n = 1.4 kDa were formed. On the other hand, acetone has intermediate hydrogen bonding accepting ability and optimal intermediate polymer-solvent interactions and, therefore, an intermediate enzymatic rate constant of approximately 0.41-0.52 L mol -1 h -1 , and the highest molar mass polymers with M n = 4.9-9.4 kDa were obtained.