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

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

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
Volume83
Issue number3
DOIs
Publication statusPublished - Mar 1 2006

Fingerprint

lauric acid
Lipases
Esterification
Lipase
Membranes
Acids
Fibers
Anions
Ion exchange
Negative ions
Benzyl Alcohol

All Science Journal Classification (ASJC) codes

  • Chemical Engineering(all)
  • Organic Chemistry

Cite this

Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane. / Goto, Muneharu; Kawakita, Hidetaka; Uezu, Kazuya; Tsuneda, Satoshi; Saito, Kyoichi; Goto, Masahiro; Tamada, Masao; Sugo, Takanobu.

In: JAOCS, Journal of the American Oil Chemists' Society, Vol. 83, No. 3, 01.03.2006, p. 209-213.

Research output: Contribution to journalArticle

Goto, Muneharu ; Kawakita, Hidetaka ; Uezu, Kazuya ; Tsuneda, Satoshi ; Saito, Kyoichi ; Goto, Masahiro ; Tamada, Masao ; Sugo, Takanobu. / Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane. In: JAOCS, Journal of the American Oil Chemists' Society. 2006 ; Vol. 83, No. 3. pp. 209-213.
@article{047ee15c99a84c90992b99dbbec74ccc,
title = "Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane",
abstract = "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.",
author = "Muneharu Goto and Hidetaka Kawakita and Kazuya Uezu and Satoshi Tsuneda and Kyoichi Saito and Masahiro Goto and Masao Tamada and Takanobu Sugo",
year = "2006",
month = "3",
day = "1",
doi = "10.1007/s11746-006-1195-x",
language = "English",
volume = "83",
pages = "209--213",
journal = "Oil & Soap",
issn = "0003-021X",
publisher = "Springer Verlag",
number = "3",

}

TY - JOUR

T1 - Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane

AU - Goto, Muneharu

AU - Kawakita, Hidetaka

AU - Uezu, Kazuya

AU - Tsuneda, Satoshi

AU - Saito, Kyoichi

AU - Goto, Masahiro

AU - Tamada, Masao

AU - Sugo, Takanobu

PY - 2006/3/1

Y1 - 2006/3/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=33646251641&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33646251641&partnerID=8YFLogxK

U2 - 10.1007/s11746-006-1195-x

DO - 10.1007/s11746-006-1195-x

M3 - Article

VL - 83

SP - 209

EP - 213

JO - Oil & Soap

JF - Oil & Soap

SN - 0003-021X

IS - 3

ER -