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Title: ESTERIFICATION AND ALCOHOLYSIS ACTIVITY OF IMMOBILIZED LIPASES

Author
item Foglia, Thomas
item Jones, Kerby
item Marmer, William

Submitted to: Annual Meeting and Expo of the American Oil Chemists' Society
Publication Type: Abstract Only
Publication Acceptance Date: 2/5/2005
Publication Date: 5/1/2005
Citation: Foglia, T.A., Jones, K.C., Marmer, W.N. 2005. Esterification and alcoholysis activity of immobilized lipases [abstract]. Annual Meeting and Expo of the American Oil Chemists' Society. p. 15.

Interpretive Summary:

Technical Abstract: Immobilized lipases were screened for their ability to catalyze the alcoholysis of greases to their simple alkyl ester derivatives. The immobilized lipases studied included: Pseudomonas burkholderia (P. b.), Thermomyces lanuguinosa (T. l.) and Rhizomucor miehei (R. m.). All the immobilized lipases were used to catalyze alkyl ester formation from various fats or oils having a range of free fatty acid (FFA) content (2.6 to 36%). Their relative esterification and transesterification activities were determined. Alcoholysis reactions were carried out at 50 C at a triacylglycerol to alcohol mole ratio of 1 to 4 in solvent and solvent-free systems. For equal amounts of protein used, the immobilized T. l. and R. m. lipases exhibited faster rates of alkyl ester production than the immobilized P. b. lipase for both FFA esterification and glyceride alcoholysis. The immobilized T l. and R. m. lipases had similar activity and were more effective in catalyzing ester synthesis than the immobilized P. b. lipase. The alcoholysis activity of the T. l. lipase immobilized on granulated silica also was compared with the same lipase supported within a phyllosilicate sol gel. Under the same conditions, phyllosilicate-immobilized T. l. was more active than granulated T. l., but had the same activity as that of phyllosilicate-immobilized P. b. The addition of molecular sieves increased alkyl ester synthesis in reactions catalyzed by immobilized P. b. but did not improve ester yields when using the T. l. or R. m. lipases.