Enhanced stability and decolorization of coomassie brilliant blue R-250 by dextran aldehyde-modified horseradish peroxidase

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Abstract

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. Copyright © 2011 Informa Healthcare USA, Inc.

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Altikatoglu, M., & Celebi, M. (2011). Enhanced stability and decolorization of coomassie brilliant blue R-250 by dextran aldehyde-modified horseradish peroxidase. Artificial Cells, Blood Substitutes, and Biotechnology, 39(3), 185–190. https://doi.org/10.3109/10731199.2010.533124

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