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.

Full Text: PDF DOI: 10.5539/ijc.v2n2p77

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International Journal of Chemistry   ISSN 1916-9698 (Print)   1916-9701 (Online)

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