R. Rosu et al., REPEATED USE OF IMMOBILIZED LIPASE FOR MONOACYLGLYCEROL PRODUCTION BYSOLID-PHASE GLYCEROLYSIS OF OLIVE OIL, Journal of the American Oil Chemists' Society, 74(4), 1997, pp. 445-450
By using immobilized lipase for production of monoacylglycerol (MAG) b
y solid-phase glycerolysis of fats and oils, the enzyme could be recov
ered easily from the reaction mixture and recycled to reduce the cost
of the catalyst. Several support materials (CaCO3, CaSO4 . 2H(2)O, Ca2
P2O7, and Celite) were screened for immobilization of Pseudomonas sp.
lipase by adsorption and tested for solid-phase glycerolysis of olive
oil. Immobilization made the reuse of enzyme feasible. CaCO proved to
be the best support: 90% MAC (wt% in the glycerol-free reaction mixtur
e after 72 h of reaction rime) was obtained until the fifth use, 80% a
fter the seventh use, and 60% after the tenth use. The same support wa
s found suitable for immobilization of two other bacterial lipases fro
m Chromobacterium viscosum and Pseudomonas pseudoalkali.