Enhanced Stability and Decolorization of Coomassie Brilliant Blue R-250 by Dextran Aldehyde-modified Horseradish Peroxidase

被引：15

作者：

Altikatoglu, Melda ^{[1
]}

Celebi, Mithat ^{[2
]}

机构：

[1] Yildiz Tech Univ, Fac Arts & Sci, Dept Chem, TR-34210 Istanbul, Turkey

[2] Yalova Univ, Dept Polymer Engn, Fac Engn, Yalova, Turkey

来源：

ARTIFICIAL CELLS BLOOD SUBSTITUTES AND BIOTECHNOLOGY | 2011年 / 39卷 / 03期

关键词：

HRP; dextran aldehyde; modification; Coomassie Brilliant Blue R-250; decolorization; AZO-DYE; INTERFACIAL INACTIVATION; TEXTILE; DEGRADATION; REMOVAL; OXIDASE; IMMOBILIZATION; NANOPARTICLES; TEMPERATURE; EFFLUENT;

D O I：

10.3109/10731199.2010.533124

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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.

引用

页码：185 / 190

页数：6

共 39 条

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