Lipase‐mediated acidolysis of tristearin with CLA in a packed‐bed reactor: A kinetic study

Solvent‐free acidolysis of tristearin with CLA has been carried out in a packed‐bed reactor. An immobilized lipase from Thermomyces lanuginosa (Lipozyme TL IM) was employed as the biocatalyst. Elevated temperatures (75°C) were utilized to eliminate solid substrates. The reaction kinetics were modeled by using a rate equation of the general Michaelis‐Menten form. Both the extent of incorporation of CLA and the extent to which FFA were released were investigated. Positional analysis of the purified TAG obtained after a pseudo space time of 0.6 h indicated that CLA was preferentially incorporated at the sn‐1,3 positions of the glycerol backbone, although 10% of the sn‐2 positions were occupied by CLA residues. At a pseudo space time of 0.6 h, 38% of the initial CLA was incorporated in acylglycerols; the associated extent of hydrolysis was 8.3%.