Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane

Muneharu Goto*, Hidetaka Kawakita, Kazuya Uezu, Satoshi Tsuneda, Kyoichi Saito, Masahiro Goto*, Masao Tamada, Takanobu Sugo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


A porous anion-exchange hollow-fiber membrane was prepared by radiation-induced graft polymerization and chemical modification to immobilize lipase for enzymatic reaction in an organic solvent. The amount of anion-exchange group introduced to the porous hollow-fiber membrane was 2.5 mol/kgfiber. A lipase solution was allowed to permeate through the porous anion-exchange hollow-fiber membrane, and lipase molecules that adsorbed onto the grafted polymer brush were cross-linked with glutaraldehyde. The lipase was immobilized at a density of 0.14 kglipase/kgfiber, which was equivalent to a degree of multilayer binding of 20. Esterification was carried out by passing a solution of lauric acid and benzyl alcohol in anhydrous isooctane through the lipase-immobilized membrane, and lipase activity was determined. A reaction percentage of 50% was achieved at space velocity 68 h-1. The maximum immobilized lipase and native lipase activities were 8.9 and 0.38 mol/(h·kglipase), respectively. Thus, the activity of the immobilized lipase was 23.4 times higher than that of the native lipase.

Original languageEnglish
Pages (from-to)209-213
Number of pages5
JournalJAOCS, Journal of the American Oil Chemists' Society
Issue number3
Publication statusPublished - 2006 Mar


  • Enzymatic esterification
  • Graft polymerization
  • Hollow-fiber
  • Immobilization
  • Lauric acid
  • Lipase
  • Polymer brush
  • Rhizopus sp

ASJC Scopus subject areas

  • General Chemical Engineering
  • Organic Chemistry


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