Bulletin of the Chemical Society of Japan p. 2411 - 2420 (1992)
Update date:2022-08-16
Topics:
Okahata, Yoshio
Ijiro, Kuniharu
A lipid-coated lipase was prepared by mixing aqueous solutions of lipase and dialkyl amphiphiles: A hydrophilic surface of the enzyme is converted with a lipid layer, of which lipophilic two-long-alkyl tails solubilize the enzyme in hydrophobic organic solvents.The lipid-coated lipase was prepared in various conditions by changing hydrophilic head groups of lipid molecules, a ratio of lipid/lipase, and an origin of lipase; the complex prepared from nonionic amphiphiles and lipase D from Rhizopus delemar showed a high stability and a high enzymatic activity in hydrophobic organic solutions.The lipid-coated lipase catalyzed di- and triacylglycerol syntheses from monoacylglycerols and aliphatic acids in the homogeneous and dry benzene solution in the presence of two pieces of molecular sieves (water: 80 ppm). the lipid-coated lipase could also catalyze ester exchange reactions in organic solvents with a small amount of water (250 ppm).Enzymatic activity was effected by a nature of organic solvents and a water content in organic solvents.The catalytic activity of the lipid-coated lipase was highly efficient compared with other enzyme systems such as the poly(ethylene glycol)-grafted lipase and the direct dispersion of lipase powder for glyceride syntheses in the dry organic solution.
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