Design of polymer brushes for immobilizing enzymes onto hollow fiber micropores in organic media reaction

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

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

To immobilize lipase for enzymatic reactions in organic solvent, various functional [epoxy (GMA-fiber), hydroxyl (OH-fiber) or diethyl amino (DEA-fiber)] groups were introduced onto porous hollow-fiber membranes by radiation-induced graft polymerization of glycidyl methacrylate and chemical modification. Lipase from Candida rugosa was immobilized on polymer brushes by permeation of lipase. The activities of immobilized lipase were measured by esterification reactions between lauric acid and benzyl alcohol in isooctane. The activity of immobilized lipase on GMA-fibers, DEA-fibers and OH-fibers was 0.70 mol/(h kg-lipase), 0.50 mol/(h kg-lipase), and 2.45 mol/(h kg-lipase), respectively. Immobilized lipase on DEA-fibers or OH-fibers was reused three times after it was used in the batch reactor for 24 h. It was found that lipase activity showed no signs of denaturation. However, when native lipase was used, lipase activity remarkably decreased after reusing.

Original languageEnglish
Pages (from-to)159-165
Number of pages7
JournalBiochemical Engineering Journal
Volume37
Issue number2
DOIs
Publication statusPublished - Nov 15 2007

Fingerprint

Lipases
Brushes
Lipase
Polymers
Enzymes
Fibers
lauric acid
Benzyl Alcohol
Denaturation
Candida
Esterification
Chemical modification
Batch reactors
Grafts
Permeation
Polymerization
Hydroxyl Radical
Organic solvents
Alcohols
Thermodynamic properties

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Environmental Engineering
  • Biomedical Engineering

Cite this

Design of polymer brushes for immobilizing enzymes onto hollow fiber micropores in organic media reaction. / Goto, Muneharu; Okubo, Tokie; Kawakita, Hidetaka; Uezu, Kazuya; Tsuneda, Satoshi; Saito, Kyoichi; Goto, Masahiro; Tamada, Masao; Sugo, Takanobu.

In: Biochemical Engineering Journal, Vol. 37, No. 2, 15.11.2007, p. 159-165.

Research output: Contribution to journalArticle

Goto, M, Okubo, T, Kawakita, H, Uezu, K, Tsuneda, S, Saito, K, Goto, M, Tamada, M & Sugo, T 2007, 'Design of polymer brushes for immobilizing enzymes onto hollow fiber micropores in organic media reaction', Biochemical Engineering Journal, vol. 37, no. 2, pp. 159-165. https://doi.org/10.1016/j.bej.2007.04.008
Goto, Muneharu ; Okubo, Tokie ; Kawakita, Hidetaka ; Uezu, Kazuya ; Tsuneda, Satoshi ; Saito, Kyoichi ; Goto, Masahiro ; Tamada, Masao ; Sugo, Takanobu. / Design of polymer brushes for immobilizing enzymes onto hollow fiber micropores in organic media reaction. In: Biochemical Engineering Journal. 2007 ; Vol. 37, No. 2. pp. 159-165.
@article{f13f431fbb5143d8af324ab5bead7b74,
title = "Design of polymer brushes for immobilizing enzymes onto hollow fiber micropores in organic media reaction",
abstract = "To immobilize lipase for enzymatic reactions in organic solvent, various functional [epoxy (GMA-fiber), hydroxyl (OH-fiber) or diethyl amino (DEA-fiber)] groups were introduced onto porous hollow-fiber membranes by radiation-induced graft polymerization of glycidyl methacrylate and chemical modification. Lipase from Candida rugosa was immobilized on polymer brushes by permeation of lipase. The activities of immobilized lipase were measured by esterification reactions between lauric acid and benzyl alcohol in isooctane. The activity of immobilized lipase on GMA-fibers, DEA-fibers and OH-fibers was 0.70 mol/(h kg-lipase), 0.50 mol/(h kg-lipase), and 2.45 mol/(h kg-lipase), respectively. Immobilized lipase on DEA-fibers or OH-fibers was reused three times after it was used in the batch reactor for 24 h. It was found that lipase activity showed no signs of denaturation. However, when native lipase was used, lipase activity remarkably decreased after reusing.",
author = "Muneharu Goto and Tokie Okubo and Hidetaka Kawakita and Kazuya Uezu and Satoshi Tsuneda and Kyoichi Saito and Masahiro Goto and Masao Tamada and Takanobu Sugo",
year = "2007",
month = "11",
day = "15",
doi = "10.1016/j.bej.2007.04.008",
language = "English",
volume = "37",
pages = "159--165",
journal = "Biochemical Engineering Journal",
issn = "1369-703X",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Design of polymer brushes for immobilizing enzymes onto hollow fiber micropores in organic media reaction

AU - Goto, Muneharu

AU - Okubo, Tokie

AU - Kawakita, Hidetaka

AU - Uezu, Kazuya

AU - Tsuneda, Satoshi

AU - Saito, Kyoichi

AU - Goto, Masahiro

AU - Tamada, Masao

AU - Sugo, Takanobu

PY - 2007/11/15

Y1 - 2007/11/15

N2 - To immobilize lipase for enzymatic reactions in organic solvent, various functional [epoxy (GMA-fiber), hydroxyl (OH-fiber) or diethyl amino (DEA-fiber)] groups were introduced onto porous hollow-fiber membranes by radiation-induced graft polymerization of glycidyl methacrylate and chemical modification. Lipase from Candida rugosa was immobilized on polymer brushes by permeation of lipase. The activities of immobilized lipase were measured by esterification reactions between lauric acid and benzyl alcohol in isooctane. The activity of immobilized lipase on GMA-fibers, DEA-fibers and OH-fibers was 0.70 mol/(h kg-lipase), 0.50 mol/(h kg-lipase), and 2.45 mol/(h kg-lipase), respectively. Immobilized lipase on DEA-fibers or OH-fibers was reused three times after it was used in the batch reactor for 24 h. It was found that lipase activity showed no signs of denaturation. However, when native lipase was used, lipase activity remarkably decreased after reusing.

AB - To immobilize lipase for enzymatic reactions in organic solvent, various functional [epoxy (GMA-fiber), hydroxyl (OH-fiber) or diethyl amino (DEA-fiber)] groups were introduced onto porous hollow-fiber membranes by radiation-induced graft polymerization of glycidyl methacrylate and chemical modification. Lipase from Candida rugosa was immobilized on polymer brushes by permeation of lipase. The activities of immobilized lipase were measured by esterification reactions between lauric acid and benzyl alcohol in isooctane. The activity of immobilized lipase on GMA-fibers, DEA-fibers and OH-fibers was 0.70 mol/(h kg-lipase), 0.50 mol/(h kg-lipase), and 2.45 mol/(h kg-lipase), respectively. Immobilized lipase on DEA-fibers or OH-fibers was reused three times after it was used in the batch reactor for 24 h. It was found that lipase activity showed no signs of denaturation. However, when native lipase was used, lipase activity remarkably decreased after reusing.

UR - http://www.scopus.com/inward/record.url?scp=35248852814&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35248852814&partnerID=8YFLogxK

U2 - 10.1016/j.bej.2007.04.008

DO - 10.1016/j.bej.2007.04.008

M3 - Article

VL - 37

SP - 159

EP - 165

JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

SN - 1369-703X

IS - 2

ER -