TY - JOUR
T1 - Strategies for lipase-catalyzed production and the purification of structured phospholipids
AU - Vikbjerg, Anders Falk
AU - Rusig, J.-Y.
AU - Jonsson, Gunnar
AU - Mu, Huiling
AU - Xu, X.
PY - 2006/1/1
Y1 - 2006/1/1
N2 - This work provides different strategies for the enzymatic modification of the fatty acid composition in soybean phosphatidylcholine (PC) and the subsequent purification. Enzymatic transesterification reactions with caprylic acid as acyl donor were carried out in continuous enzyme bed reactors with a commercial immobilized lipase (Lipozyme RM IM) as catalyst. Operative stability of the immobilized lipase was examined under solvent and solvent-free conditions. The long reaction time required to have a high incorporation, combined with rapid deactivation of the enzyme, makes the solvent-free transesterification reaction unfavorable. Performing the reaction in the presence of solvent (hexane) makes it possible to have high incorporation into PC and deactivation of the lipase is less pronounced as compared to solvent-free operations. For solvent-free operation, it is suggested to recycle the reaction mixture through the packed bed reactor, as this would increase incorporation of the desired fatty acids, due to increased contact time between substrate and enzyme in the column. Removal of free fatty acids from the reaction mixture can be done by ultrafiltration; however, parameters need to be selected with care in order to have a feasible process. No changes are observed in the phospholipid (PL) distribution during ultrafiltration, and other techniques as column chromatography may be required if high purity of individual PL species is desired. LC/MS analysis of transesterified PC revealed the presence of 8:0/8:0-PC, showing that acyl migration takes place during the acidolysis reaction.
AB - This work provides different strategies for the enzymatic modification of the fatty acid composition in soybean phosphatidylcholine (PC) and the subsequent purification. Enzymatic transesterification reactions with caprylic acid as acyl donor were carried out in continuous enzyme bed reactors with a commercial immobilized lipase (Lipozyme RM IM) as catalyst. Operative stability of the immobilized lipase was examined under solvent and solvent-free conditions. The long reaction time required to have a high incorporation, combined with rapid deactivation of the enzyme, makes the solvent-free transesterification reaction unfavorable. Performing the reaction in the presence of solvent (hexane) makes it possible to have high incorporation into PC and deactivation of the lipase is less pronounced as compared to solvent-free operations. For solvent-free operation, it is suggested to recycle the reaction mixture through the packed bed reactor, as this would increase incorporation of the desired fatty acids, due to increased contact time between substrate and enzyme in the column. Removal of free fatty acids from the reaction mixture can be done by ultrafiltration; however, parameters need to be selected with care in order to have a feasible process. No changes are observed in the phospholipid (PL) distribution during ultrafiltration, and other techniques as column chromatography may be required if high purity of individual PL species is desired. LC/MS analysis of transesterified PC revealed the presence of 8:0/8:0-PC, showing that acyl migration takes place during the acidolysis reaction.
UR - http://www.scopus.com/inward/record.url?scp=33750506906&partnerID=8YFLogxK
U2 - 10.1002/ejlt.200600138
DO - 10.1002/ejlt.200600138
M3 - Journal article
AN - SCOPUS:33750506906
SN - 1438-7697
VL - 108
SP - 802
EP - 811
JO - European Journal of Lipid Science and Technology
JF - European Journal of Lipid Science and Technology
IS - 10
ER -