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High Conversion in Asymmetric Hydrolysis during Permeation through Enzyme‐Multilayered Porous Hollow‐Fiber Membranes
Author(s) -
Kawai Tomomi,
Nakamura Masanori,
Sugita Kazuyuki,
Saito Kyoichi,
Sugo Takanobu
Publication year - 2001
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp010066d
Subject(s) - membrane , permeation , glycidyl methacrylate , adsorption , hollow fiber membrane , fiber , polymerization , chemistry , chemical engineering , glutaraldehyde , polymer chemistry , polymer , materials science , chromatography , organic chemistry , biochemistry , engineering
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.