Enhanced stability and decolorization of Coomassie Brilliant Blue R-250 by dextran aldehyde-modified horseradish peroxidase.

Melda Altikatoglu, Mithat Celebi
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引用次数: 17

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.

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葡聚糖醛修饰的辣根过氧化物酶提高考马斯亮蓝R-250的稳定性和脱色效果。
用高碘酸活化的葡聚糖对辣根过氧化物酶(EC 1.11.1.7)进行化学修饰。测定了游离酶和修饰酶对有机-水界面和某些化学物质的活性。改性后的HRP在有机溶剂中保持充分活性4小时。然而,未改性的酶在前2小时内失去50%的活性。研究了可能的抑制剂对酶活性的影响。此外,comasassie Brilliant Blue R-250使用自由和改性HRP有效脱色。处理5分钟后,染料脱色率为80-90%。与游离HRP相比,改性HRP表现出了更好的性能。
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