ACTIVITY AND STABILITY OF LIPASE IN THE SOLID-PHASE GLYCEROLYSIS OF TRIOLEIN

Lipase-catalyzed glycerolysis of triolein was studied in a solid-phase system The activity and stability of three bacterial lipases in crude and purified forms were examined. Most of these lipases were suitable for the high-yield synthesis of monooleylglycerol. With crude lipase from Chromobacterium viscosum, 96% monooleylglycerol concentration was achieved. In the case of pure lipase from Pseudomonas cepacia, immobi lization on Celite was necessary. This led to a strong increase in the long-term stability and final monooleylglycerol concentration. Immobi lization on Sepharose(TX) led to less stable and active lipases from P . cepacia. In general the highest loss in stability was observed in th e first reaction hour, and purified lipases were less suitable. Furthe rmore, sir yeast and mold lipases were employed as catalysts in the mo del reaction system. Most of them have been neither very stable nor ve ry active in the glycerolysis reaction. Only purified lipase from Rhiz opus delemar gave moderate,monooleylglycerol concentrations. The addit ion of a. delemar at intervals influenced neither stability nor monool eylglycerol concentrations. The optimum cooling temperature for the so lidification of the reaction mixture, which was necessary for high mon ooleylglycerol concentration, was determined to be 8 degrees C.