Kinetic Studies on Lipase-catalyzed Transesterification of Phosphatidylcholine with ?-linolenic Acid Ethyl Ester
- Junmin Du
- Dong Wu
- Xianglin Hou
- Cuiping Feng
Abstract
The kinetics of the transesterification of phosphatidylcholine (PC) with ?-linolenic acid ethyl ester (ALAEE)catalyzed by immobilized lipase in hexane was studied. The reaction proceeded via a Ping-Ping Bi-Bi
mechanism without inhibition by both the substrates at various concentrations tested. A reaction kinetic model
was proposed with the experimental data. The kinetic constants of the model were determined at 45 oC, which
were 1.2×10-2 ?mol.min-1.mg-1, 64.1 mM and 282.8 mM for Vmax, KmALA and KmPC, respectively.
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- DOI:10.5539/ijc.v2n2p77
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