Studies on the activity and stability of immobilized horseradish peroxidase on poly(ethylene terephthalate) grafted acrylamide fiber.
Having been activated with glutaraldehyde, modified poly(ethylene terephthalate) grafted acrylamide fiber was used for the immobilization of horseradish peroxidase (HRP). Both the free HRP and the immobilized HRP were characterized by determining the activity profile as a function of pH, temperature, thermal stability, effect of organic solvent and storage stability. The optimum pH values of the enzyme activity were found as 8 and 7 for the free HRP and the immobilized HRP respectively. The temperature profile of the free HRP and the immobilized HRP revealed a similar behaviour, although the immobilized HRP exhibited higher relative activity in the range from 50 to 60 degrees C. The immobilized HRP showed higher storage stability than the free HRP.
Department of Chemistry, Faculty of Science and Arts, Kirikkale University, 71450, Kirikkale, Turkey.
Zülfikar
Z
Temoçin
Mustafa
M
Yiğitoğlu
D000180:Acrylic Resins; D001709:Biotechnology; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011092:Polyethylene Glycols; D011093:Polyethylene Terephthalates; D012997:Solvents; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics; D000099166:Polyacrylamides
D000180:Acrylic Resins; D004800:Enzymes, Immobilized; D006735:Horseradish Peroxidase; D011092:Polyethylene Glycols; D011093:Polyethylene Terephthalates; D012997:Solvents; D000099166:Polyacrylamides