Functionalization of catalase for a photochemical immobilization on poly(ethylene terephthalate).
The enzyme catalase (EC 1.11.1.6) was covalently immobilized on textile carrier fabrics made of poly(ethylene terephthalate) (PET) by a novel combined wet chemical and photochemical process. The functionalization of catalase with allyl groups succeeds in a wet chemical treatment of the enzyme with allylglycidylether. This modified enzyme was bonded covalently to the textile material by a photochemical immobilization using a monochromatic excimer UV lamp (222 nm). Using this two-step procedure nearly 60 mg enzyme/g carrier could be fixed durably. The efficiency of the immobilization products was investigated by measuring the enzymatic decomposition of hydrogen peroxide in comparison to the free enzyme. The relative activity of the catalase after the immobilization was nearly 5% compared to the free, not fixed enzyme; however, even after 30 reuses, the modified and immobilized catalase still showed a distinct activity.
Opwis
Klaus
K
Deutsches Textilforschungszentrum Nord-West e.V., Krefeld, Germany. opwis@dtnw.de
Knittel
Dierk
D
Schollmeyer
Eckhard
E
D002374:Catalase / Q000737:chemistry / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D008855:Microscopy, Electron, Scanning; D010777:Photochemistry / Q000379:methods; D011091:Polyesters / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry*; D011093:Polyethylene Terephthalates; D013784:Textiles / Q000032:analysis / Q000528:radiation effects; D014466:Ultraviolet Rays
D004800:Enzymes, Immobilized; D011091:Polyesters; D011093:Polyethylene Terephthalates; D011092:Polyethylene Glycols; D006861:Hydrogen Peroxide; D002374:Catalase