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

発表形態:
原著論文
主要業績:
主要業績
単著・共著:
共著
発表年月:
2006年
DOI:
会議属性:
査読:
有り
リンク情報:

日本語フィールド

著者:
Goto, Muneharu; Kawakita, Hidetaka; Uezu, Kazuya; Tsuneda, Satoshi; Saito, Kyoichi; Goto, Masahiro; Tamada, Masao; Sugo, Takanobu.
題名:
Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane.
発表情報:
Journal of the American Oil Chemists' Society 巻: 83 ページ: 209-213
キーワード:
lipase, radiation-induced graft polymerization, porous hollow-fiber membrane, polymer brush
概要:
抄録:
A porous anion-exchange hollow-fiber membrane was prepd. by radiation-induced graft polymn. and chem. modification to immobilize lipase for enzymic reaction in an org. solvent. The amt. of anion-exchange group introduced to the porous hollow-fiber membrane was 2.5 mol/kgfiber. A lipase soln. was allowed to permeate through the porous anion-exchange hollow-fiber membrane, and lipase mols. that adsorbed onto the grafted polymer brush were cross-linked with glutaraldehyde. The lipase was immobilized at a d. of 0.14 kglipase/kgfiber, which was equiv. to a degree of multilayer binding of 20. Esterification was carried out by passing a soln. of lauric acid and benzyl alc. in anhyd. isooctane through the lipase-immobilized membrane, and lipase activity was detd. A reaction percentage of 50% was achieved at space velocity 68 h-1. The max. immobilized lipase and native lipase activities were 8.9 and 0.38 mol/(h⋅kglipase), resp. Thus, the activity of the immobilized lipase was 23.4 times higher than that of the native lipase.

英語フィールド

Author:
Goto, Muneharu; Kawakita, Hidetaka; Uezu, Kazuya; Tsuneda, Satoshi; Saito, Kyoichi; Goto, Masahiro; Tamada, Masao; Sugo, Takanobu.
Title:
Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane.
Announcement information:
Journal of the American Oil Chemists' Society Vol: 83 Page: 209-213
Keyword:
lipase, radiation-induced graft polymerization, porous hollow-fiber membrane, polymer brush
An abstract:
A porous anion-exchange hollow-fiber membrane was prepd. by radiation-induced graft polymn. and chem. modification to immobilize lipase for enzymic reaction in an org. solvent. The amt. of anion-exchange group introduced to the porous hollow-fiber membrane was 2.5 mol/kgfiber. A lipase soln. was allowed to permeate through the porous anion-exchange hollow-fiber membrane, and lipase mols. that adsorbed onto the grafted polymer brush were cross-linked with glutaraldehyde. The lipase was immobilized at a d. of 0.14 kglipase/kgfiber, which was equiv. to a degree of multilayer binding of 20. Esterification was carried out by passing a soln. of lauric acid and benzyl alc. in anhyd. isooctane through the lipase-immobilized membrane, and lipase activity was detd. A reaction percentage of 50% was achieved at space velocity 68 h-1. The max. immobilized lipase and native lipase activities were 8.9 and 0.38 mol/(h⋅kglipase), resp. Thus, the activity of the immobilized lipase was 23.4 times higher than that of the native lipase.


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