|Hsu, An Fei|
Submitted to: Annual Meeting and Expo of the American Oil Chemists' Society
Publication Type: Abstract Only
Publication Acceptance Date: January 15, 2004
Publication Date: May 1, 2004
Citation: Hsu, A.C., Jones, K.C., Foglia, T.A., Marmer, W.N. 2004. Transesterification activity of lipases immobilized in phyllosilicate sol-gel matrix [abstract]. 95th Annual Meeting of the American Oil Chemists' Society. p. 77. Technical Abstract: The lipases of Pseudomonas cepacia (PS-30) and Thermomyces lanuginosa (T. l.) were immobilized within a phyllosilicate sol-gel matrix and their relative esterification and transesterification activities determined. Both immobilized lipases catalyzed alkyl ester formation from various fats or oils having a range of free fatty acid content (2.6 to 36%). Immobilized T.l. (IM Tl) lipase had higher transesterification activity toward fats and oils with low amounts of free fatty acids and/or saturated triacylglycerols. For equal amounts of protein used, the IM-Tl lipase exhibited a faster rate of alkyl ester production than the immobilized PS-30 (IM PS-30) for both FFA and triacylglycerols. At extended reaction times, however, the IM PS-30 lipase gave slightly higher yields of alkyl esters. The addition of molecular sieves to the reaction media had no effect on the IM T.l. lipase-catalyzed ester yields but did improve the IM PS-30 lipase-catalyzed conversion to alkyl estrers. Time course studies of the IM PS-30 and IM T.l. lipase-catalyzed ethanolysis of various greases and fats indicated that IM T.l. lipase transesterified a broad spectrum of greases and oils regardless of the chain length or degree of unsaturation of the fatty acyl groups present, whereas the IM PS-30 lipase favored medium and long-chain acyl groups. The phyllosilicate sol-gel immobilized T.l. and PS-30 lipases have potential as catalysts for production of simple esters from fats, oils, and greases of high FFA content.