Yang_2015_J.Oleo.Sci_64_443

Reference

Title : Lysophosphatidylcholine synthesis by lipase-catalyzed ethanolysis - Yang_2015_J.Oleo.Sci_64_443
Author(s) : Yang G , Yang R , Hu J
Ref : J Oleo Sci , 64 :443 , 2015
Abstract :

Lysophosphatidylcholine (LPC) is amphiphilic substance, and possesses excellent physiological functions. In this study, LPC was prepared through ethanolysis of phosphatidylcholine (PC) in n-hexane or solvent free media catalyzed by Novozym 435 (from Candida antarctica), Lipozyme TLIM (from Thermomcyces lanuginosus) and Lipozyme RMIM (from Rhizomucor miehei). The results showed that three immobilized lipases from Candida Antarctica, Thermomcyces lanuginosus and Rhizomucor miehei could catalyze ethanolysis of PC efficiently. In n-hexane, the LPC conversions of ethanolysis of PC catalyzed by Novozyme 435, Lipozyme TLIM and Lipozyme RMIM could reach to 98.5 +/- 1.6%, 94.6 +/- 1.4% and 93.7 +/- 1.8%, respectively. In solvent free media, the highest LPC conversions of ethanolysis of PC catalyzed by Novozyme 435, Lipozyme TL IM and Lipozyme RM IM were 97.7 +/- 1.7%, 93.5 +/- 1.2% and 93.8 +/- 1.9%, respectively. The catalytic efficiencies of the three lipases were in the order of Novozyme 435 > Lipozyme TLIM > Lipozyme RMIM. Furthermore, their catalytic efficiencies in n-hexane were better than those in solvent free media.

PubMedSearch : Yang_2015_J.Oleo.Sci_64_443
PubMedID: 25766935

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Citations formats

Yang G, Yang R, Hu J (2015)
Lysophosphatidylcholine synthesis by lipase-catalyzed ethanolysis
J Oleo Sci 64 :443

Yang G, Yang R, Hu J (2015)
J Oleo Sci 64 :443