Abstract
Lysophosphatidylcholines (LPC) were synthesized from l-α-glycerophosphatidylcholine (GPC) by lipase-catalyzed esterification in a solvent-free system. Adding small amounts of a water-mimicking solvent such as dimethylformamide (DMF) to the reaction media significantly enhanced the reaction rate and the product yield. The role of solvent was studied with regard to changes in substrate solubility, the water activity of the reaction system, and the water content of the enzyme. Whereas the solubility of GPC was virtually unaffected by the addition of DMF at controlled water activity, it was considerably affected by water activity. DMF itself lowered the water activity of the system and deprived Lipozyme IM of water. The LPC production was also controlled by varying the initial water content of the enzyme. When two kinds of controls were employed together, a synergistic effect was observed and a 90% conversion was achieved. As a result, an operating window was suggested for LPC production, including water activity of Lipozyme IM and concentration of DMF as two parameters.
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References
Aoi, N., Soy Lysolecithin, Yukagaku 39:10–15 (1990).
Fujita, S., and K. Suzuki, Surface Activity of the Lipid Products Hydrolyzed with Lipase and Phospholipase A-2, J. Am. Oil Chem. Soc. 67:1008–1014 (1990).
Nakai, E., K. Suzuki, S. Sato, and M. Kato, Enzymic Hydrolysis of Phospholipids, Jpn. Kokai Tokkyo Koho JP 63,44,893 (1988).
Kudo, S., and E. Nishi, Surfactant and Process for Producing the Same, PCT International Appl. WO 90 11,823 (1990).
Yesair, D.W., Methods for Making Lysophosphatidylcholine, Ibid. PCT International Appl. WO 97 28,270 (1997).
Kim, J.-K., M.-K. Kim, G.-H. Chung, C.-S. Choi, and J.-S. Rhee, Production of Lysophospholipid Using Extracellular Phospholipase A1 from Serratia sp. MK1, J. Microbiol. Biotechnol. 7:258–261 (1997).
Haas, M.J., K. Scott, and G. Janssen, Enzymatic Phosphatidylcholine Hydrolysis in Organic Solvents: An Examination of Selected Commercially Available Lipases, J. Am. Oil Chem. Soc. 71:483–490 (1994).
Sarney, D.B., G. Fregapane, and E.N. Vulfson, Lipase-Catalyzed Synthesis of Lysophospholipids in a Continuous Bioreactor, ——Ibid. 71:93–96 (1994).
Mustranta, A., P. Forssel, and K. Poutanen, Comparison of Lipases and Phospholipases in the Hydrolysis of Phospholipids, Process Biochem. 30:393–401 (1995).
Maeda, K., N. Kawamoto, and T. Ishida, Manufacture of Lysophospholipids with Lipase, Jpn. Kokai Tokkyo Koho JP 02,107,195 (1990).
Han, J.J., and J.S. Rhee, Effect of Salt Hydrate Pairs for Water Activity Control on Lipase-Catalyzed Synthesis of Lysophospholipids in a Solvent-Free System, Enzyme Microb. Technol. 22:158–164 (1998).
Kim, J., and B.G. Kim, Lipase-Catalyzed Synthesis of Lysophosphatidylcholine, Ann. NY Acad. Sci. 864:341–344 (1998).
Virto, C., I. Svensson, and P. Adlercreutz, Enzymatic Synthesis of Lysophosphatidic Acid and Phosphatidic Acid, Enzyme Microb. Technol. 24:651–658 (1999).
Mazur, A.W., G.D. Hiler II, S.S.C. Lee, M.P. Armstrong, and J.D. Wendel, Regio- and Stereoselective Enzymatic Esterification of Glycerol and Its Derivatives, Chem. Phys. Lipids 60: 189–199 (1991)
Christie, W.W., Lipid Analysis, Pergamon Press, Oxford, 1982, p. 119.
Henderson, R.J., and D.R. Tocher, Thin-Layer Chromatography, in Lipid Analysis: A Practical Approach, edited by R.J. Hamilton and S. Hamilton, Oxford University Press, 1992, pp. 65–111.
Valivety, R.H., P.J. Halling, and A.R. Macrae, Reaction Rate with Suspended Lipase Catalyst Shows Similar Dependence on Water Activity in Different Organic Solvents, Biochim. Biophys. Acta 1118:218–222 (1992).
Svensson, I., E. Wehtje, P. Adlercreutz, and B. Mattiasson, Effects of Water Activity on Reaction Rates and Equilibrium Positions in Enzymatic Esterifications, Biotechnol. Bioeng. 44: 549–556 (1994).
Bello, J.F., E. Llama, C. del Campo, M.J. Cabezas, J.V. Sinisterra, and M.S. Arias, Structure Activity Relationship in the Hydrolysis of N-Benzoylphenylalanine Esters Catalyzed by α-Chymotrypsin, J. Mol. Cat. 78:91–112 (1993).
Colombié, S., R.J. Tweddell, J.S. Condoret, and A. Marty, Water Activity Control: A Way to Improve the Efficiency of Continuous Lipase Esterification, Biotechnol. Bioeng. 60: 362–368 (1998).
Gorman, L.A.S., and J.S. Dordick, Organic Solvents Strip Water Off Enzymes, Biotechnol. Bioeng. 39:392–397 (1992).
Coulon, D., M. Girardin, B. Rovel, and M. Ghoul, Comparison of Direct Esterification and Transesterification of Fructose by Candida antarctica Lipase, Biotechnol. Lett. 17:183–186 (1995).
Yang, F., T.W. Weber, J.L. Gainer, and G. Carta, Synthesis of Lovastatin with Immobilized Candida rugosa Lipase in Organic Solvent: Effect of Reaction Conditions on Initial Rates, Biotechnol. Bioeng. 56:671–680 (1997).
Woodley, J.M., and N.J. Titchener-Hooker, The Use of Windows of Operation as a Bioprocess Design Tool, Bioprocess Eng. 14:263–268 (1996).
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Kim, J., Kim, BG. Lipase-catalyzed synthesis of lysophosphatidylcholine using organic cosolvent for in situ water activity control. J Amer Oil Chem Soc 77, 791–797 (2000). https://doi.org/10.1007/s11746-000-0126-1
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DOI: https://doi.org/10.1007/s11746-000-0126-1