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 - 2006 Mar

    Fingerprint

    lauric acid
    micropores
    dodecanoic acid
    Esterification
    Lipases
    esterification
    anion exchange
    Lipase
    Membranes
    Acids
    Fibers
    benzyl alcohol
    permeates
    glutaraldehyde
    enzymatic reactions
    polymerization
    polymers
    Anions
    Ion exchange
    Negative ions

    Keywords

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

    ASJC Scopus subject areas

    • Food Science
    • Chemistry (miscellaneous)

    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, 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.
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    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.",
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