Submitted to: Biotechnology Letters
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: December 20, 2001
Publication Date: July 20, 2002
Citation: HSU, A.C., JONES, K.C., FOGLIA, T.A. PHYLLOSILICATE SOL-GEL IMMOBILIZED LIPASES FOR THE FORMATION OF PARTIAL ACYLGLYCERIDES. BIOTECHNOLOGY LETTERS. 2002. V. 24. P. 1161-1165. Interpretive Summary: The glycerol molecule provides three sites for combining with fatty acids to make ester products. Common oils and fats are triesters of glycerol call triglycerides; mono-and diglycerides are partial glycerol esters that are being increasingly used as emulsifiers in both foods and pharmaceuticals. Currently there is a growing need to make mono- and diglycerides that contain specific nutritionally important fatty acids at specificed positions on the three-pronged glycerol backbone. These specific glycerides are not attainable using chemical approaches, but the needed specificity is achievable using certain lipase enzymes. Because of economic implications, however, when using enzyme approach, it is imperative that the biocatalyst be adaptable to continuous processes. In this paper, we describe the production of immobilized lipase preparations, which are more stable and reusable than the free lipases and suitable for continuous ester synthesis. This technology, therefore, has potential application in the continuous commercial production of mono- and diglycerides.
Technical Abstract: The phyllosilicate sol-gel immobilized lipase-catalyzed esterification of glycerol with short-, medium- and long-chain fatty acids was studied. It was found that lipase PS-30 (pseudomonas cepacia) and lipase F (Rhizopus oryzae) immobilized within a phyllosilicate sol-gel matrix were able to catalyze the esterification of glycerol with fatty acids (butyric, caprylic, lauric, oleic, and linoleic acid) to produce acylglycerols. The results from the above esterification reactions were compared to reactions using a commercially available immobilized lipase, IM-60. All three immobilixed lipases effectively esterified glycerol with caprylic, oleic, and linoleic acid to produce monoacylglycerols (MAG), diacylglycerols (DAG), and triacylglycerols (TAG). Time course studies showed that similar esterification reactions when catalyzed by free lipase PS-30 or lipase F were enhanced with the use of silica-supported glycerol. In contrast, the phyllosilicate sol-gel immobilized lipase PS-30-catalyzed reactions occurred at the same conversion rate when using either free or silica- supported glycerol. For the phyllosilicate sol-gel immobilized lipase F and IM 60 reactions, the use of silica-supported glycerol favor the production of DAG and TAG over MAG. All three immobilized lipases could be reused for acylglycerol production.