Kinetic Studies on Lipase-catalyzed Transesterification of Phosphatidylcholine with ?-linolenic Acid Ethyl Ester

  •  Junmin Du    
  •  Dong Wu    
  •  Xianglin Hou    
  •  Cuiping Feng    


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 ?, 64.1 mM and 282.8 mM for Vmax, KmALA and KmPC, respectively.

This work is licensed under a Creative Commons Attribution 4.0 License.
  • ISSN(Print): 1916-9698
  • ISSN(Online): 1916-9701
  • Started: 2009
  • Frequency: semiannual

Journal Metrics

h-index (December 2022): 32

i10-index (December 2022): 145

h5-index (December 2022): N/A

h5-median(December 2022): N/A

( The data was calculated based on Google Scholar Citations. Click Here to Learn More. )