Activity and stability of immobilized lipases in lipase-catalyzed modification of peanut oil

¹ Research Laboratory for Applied Chemistry and Biology (LARECBA), Abomey-Calavi Polytechnic School, Abomey-Calavi University, 01 BP 2009, Cotonou, Benin
² Faculty of Sciences and Technics, Department of Biochemistry and Cellular Biology, BP 526, Cotonou, Benin
³ Institute of Chemistry and Biochemistry, Department of Technical Chemistry and Biotechnology, University Greifswald, Soldmannstr, 16, D-17487 Greifswald, Germany

^* msoumanoufr@yahoo.fr

Received: 14 September 2004
Accepted: 17 January 2005

Abstract

Fatty acid release during lipolysis of peanut oil using microbial free and immobilized lipases in aqueous media was developed. Immobilized lipase from Rhizomucor miehei (RML) gave the best result from its ability to clive different fatty acids from peanut oil in such media. In organic solvent, interesterification of peanut oil with tricaprylin using immobilized lipases from RML, Chromobacterium viscosum (CVL) and Candida rugosa (CRL) was performed. The best substrate molar ratio of tricaprylin to peanut oil found was in the range 0.7 to 0.8. Using substrate molar ratio 0.7, high amount of structured triglyceride ST (about 35% MLM, 44% LML triglyceride fractions) was obtained with lipase from RML in n-hexane. The results found in solvent free system were in some cases quite similar to that obtained in organic solvent. In nine successive batch interesterification in solvent free medium using immobilized RML and CRL, no significant loss of amount of both produced triacylglycerol fractions until batch 7 was observed with RML.