High Conversion in Asymmetric Hydrolysis during Permeation through Enzyme-Multilayered Porous Hollow-Fiber Membranes
| Autor: | Takanobu Sugo, Kyoichi Saito, Masanori Nakamura, Tomomi Kawai, Kazuyuki Sugita |
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| Rok vydání: | 2001 |
| Předmět: |
Glycidyl methacrylate
Immobilized enzyme Permeability Amidohydrolases chemistry.chemical_compound Methionine Organic chemistry Amino Acids chemistry.chemical_classification Aminoacylase Hydrolysis technology industry and agriculture Membranes Artificial Stereoisomerism Equipment Design Buffer solution Polymer Permeation Enzymes Immobilized Cross-Linking Reagents Membrane chemistry Polymerization Chemical engineering Glutaral Biotechnology |
| Zdroj: | Biotechnology Progress. 17:872-875 |
| ISSN: | 8756-7938 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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