Ozcan_2009_Prep.Biochem.Biotechnol_39_170

Porcine pancreatic lipase (PPL), Candida rugosa lipase (CRL), and Castor bean lipase (CBL) were immobilized on celite by deposition from aqueous solution by the addition of hexane. Lipolytic performance of free and immobilized lipases were compared and optimizations of lipolytic enzymatic reactions conditions were performed by free and immobilized derivatives using olive oil as substrate. Afterwards, the influence on lipolysis of castor oil of free lipases and immobilized lipase derivatives have been studied in the case of production of ricinoleic acid. All of the lipases performances were compared and enzyme derivative was selected to be very effective on the production of ricinoleic acid by lipolysis reaction. Various reaction parameters affecting the production of ricinoleic acid were investigated with selected the enzyme derivative. The maximum ricinoleic acid yield was observed at pH 7-8, 50 degrees C, for 3 hours of reaction period with immobilized 1,3-specific PPL on celite. The kinetic constants K(m) and V(max) were calculated as 1.6 x 10(-4) mM and 22.2 mM from a Lineweaver-Burk plot with the same enzyme derivative. To investigate the operational stability of the lipase, the three step lipolysis process was repeated by transferring the immobilized lipase to a substrate mixture. As a result, the percentage of conversion after usage decreased markedly.