High conversion in asymmetric hydrolysis during permeation through enzyme-multilayered porous hollow-fiber membranes

被引:16
作者
Kawai, T
Nakamura, M
Sugita, K
Saito, K
Sugo, T
机构
[1] Japan Sci & Technol Corp, PRESTO, Inage Ku, Chiba 2630023, Japan
[2] Chiba Univ, Fac Engn, Dept Mat Technol, Inage Ku, Chiba 2638522, Japan
[3] Japan Atom Energy Res Inst, Takasaki Radiat Chem Res Estab, Gunma 3701292, Japan
关键词
D O I
10.1021/bp010066d
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
We describe a novel porous hollow-fiber support for immobilizing aminoacylase in multilayers. Epoxy-group-containing polymer chains were grafted onto a porous hollow-fiber membrane by radiation-induced graft polymerization of glycidyl methacrylate, and subsequently a diethylamino group as an anion-exchange group was introduced into the graft chain. Aminoacylase was adsorbed in multilayers by allowing the amioacylase buffer solution to permeate through the pores across the hollow fiber; the graft chains provided three-dimensional space for the enzymes because of their electrostatic repulsion. The adsorbed enzyme at a degree of multilayer binding of 15 was cross-linked with glutaraldehyde to prevent leakage. An acetyl-DL-methionine solution was allowed to permeate through the pores surrounded by the aminoacylase-immobilized graft chain. Production of L-methionine was observed at a 4.1 mol/h per L of the fiber for a space velocity of 200 h(-1), defined as the flow rate of the effluent penetrating the outside surface of the hollow fiber divided by the membrane volume including the lumen.
引用
收藏
页码:872 / 875
页数:4
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