Enhanced stability and decolorization of Coomassie Brilliant Blue R-250 by dextran aldehyde-modified horseradish peroxidase.
Horseradish peroxidase (EC 1.11.1.7) was chemically modified by periodate-activated dextran. The activities of free and modified enzyme against organic-aqueous interface and some chemicals were determined. Modified HRP remained fully active in the presence of organic solvent for 4 h. However, the unmodified enzyme lost 50% of its activity within the first 2 h. The effects of possible inhibitors on enzyme activity were investigated. In addition, Coomassie Brilliant Blue R-250 was efficiently decolorized using the free and modified HRP. After 5 minutes of treatment, the color removal of dye was 80-90%. Modified HRP showed effective performance compared to free HRP.
Yildiz Technical University, Faculty of Arts and Sciences, Department of Chemistry, Istanbul, Turkey. maltikatoglu@yahoo.com
Melda
M
Altikatoglu
Mithat
M
Celebi
D031215:Armoracia / Q000201:enzymology; D001673:Biodegradation, Environmental; D003911:Dextrans / Q000737:chemistry*; D004795:Enzyme Stability; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism; D012394:Rosaniline Dyes / Q000737:chemistry*; D014873:Water Pollutants / Q000737:chemistry
D003911:Dextrans; D010940:Plant Proteins; D012394:Rosaniline Dyes; D014873:Water Pollutants; C026948:dextran dialdehyde; C024757:Coomassie brilliant blue R; D006735:Horseradish Peroxidase