title: Immobilized horseradish peroxidase as a reusable catalyst for emulsion polymerization.
abstract: The study on the adsorption of horseradish peroxidase (HRP) onto silicon wafers was carried out by means of in situ ellipsometry, atomic force microscopy (AFM) and contact angle measurements. A smooth HRP layer adsorbed onto Si wafers. The enzymatic activity of free or adsorbed HRP was determined by the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and by the emulsion polymerization of ethylene glycol dimethacrylate (EGDMA). Upon adsorbing, HRP molecules might have undergone some conformational changes, which caused a small reduction of enzymatic activity in comparison to that observed for HRP solution. However, it was possible to reuse the same HRP-covered Si wafer as catalyst in the polymerization of EGDMA three times.
authors.affiliation: Instituto de Química, Universidade de São Paulo, P.O. Box 26077, São Paulo SP, 05513-970, Brazil.
authors.forename: Alliny F
authors.initials: AF
authors.lastname: Naves
authors.forename: Ana M
authors.initials: AM
authors.lastname: Carmona-Ribeiro
authors.forename: Denise F S
authors.initials: DF
authors.lastname: Petri
mesh_terms: D002384:Catalysis; D019281:Dimerization; D004655:Emulsions; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005609:Free Radicals / Q000737:chemistry / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000737:chemistry; D007700:Kinetics; D008689:Methacrylates / Q000737:chemistry; D018625:Microscopy, Atomic Force; D015394:Molecular Structure; D011108:Polymers / Q000737:chemistry*; D012825:Silicon / Q000737:chemistry
chemical_list: D004655:Emulsions; D004800:Enzymes, Immobilized; D005609:Free Radicals; D008689:Methacrylates; D011108:Polymers; C004919:ethylene dimethacrylate; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D012825:Silicon