Immobilized horseradish peroxidase as a reusable catalyst for emulsion polymerization.
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.
Naves
Alliny F
AF
Instituto de Química, Universidade de São Paulo, P.O. Box 26077, São Paulo SP, 05513-970, Brazil.
Carmona-Ribeiro
Ana M
AM
Petri
Denise F S
DF
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
D004655:Emulsions; D004800:Enzymes, Immobilized; D005609:Free Radicals; D008689:Methacrylates; D011108:Polymers; C004919:ethylene dimethacrylate; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D012825:Silicon