Esterification of lauric acid using lipase immobilized in the micropores of a hollow-fiber membrane |
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| Authors: | Muneharu Goto Hidetaka Kawakita Kazuya Uezu Satoshi Tsuneda Kyoichi Saito Masahiro Goto Masao Tamada Takanobu Sugo |
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| Affiliation: | (1) Kitakyushu National College of Technology, 5-20-1 Shii, Kokuraminami-ku, Kitakyushu, 802-0985 Fukuoka, Japan;(2) Advanced Research Institute for Science & Engineering, Kyushu Waseda University, 2-2 Hibikino, Wakamatsu-ku, Kitakyushu, 808-0135 Fukuoka, Japan;(3) Department of Chemical Processing and Environments, Faculty of Environmental Engineering, The University of Kitakyushu, 1-1 Hibikino, Wakamatsu-ku, Kitakyushu, 808-0135 Fukuoka, Japan;(4) Department of Chemical Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, 169-8555 Tokyo, Japan;(5) Faculty of Engineering, Department of Materials Technology, Chiba University, 1-33 Yayoi-cho, Inage-ku, 263-8522 Chiba, Japan;(6) Department of Materials Science and Engineering, Kyushu University, 812-8581 Fukuoka, Japan;(7) Takasaki Radiation Chemistry Research Establishment, Japan Atomic Energy Research Institute, 1233 Watanuki, Takasaki, 370-1292 Gunma, Japan |
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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 issoctane 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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| Keywords: | Enzymatic esterification graft polymerization hollow-fiber immobilization lauric acid lipase polymer brush Rhizopus sp |
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