Immobilization of horseradish peroxidase on modified chitosan beads
Immobilization of horseradish peroxidase on modified chitosan beads
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DOI：
10.1016/j.ijbiomac.2009.12.018
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发表时间：
2010-04-01
影响因子：
8.2
通讯作者：
Sarhan, A. A.
中科院分区：
文献类型：
--
作者：
Monier, M.;Ayad, D. M.;Sarhan, A. A.
以过硫酸钾和摩尔盐氧化还原引发剂为引发剂，采用接枝共聚的方法将辣根过氧化物酶固定在改性壳聚糖小球上。研究了游离和固定化HRP的活性，并用红外光谱和扫描电子显微镜对固定化HRP进行了表征。结果表明，固定化HRP的最适温度为45℃，与游离酶的最适温度相同，且固定化HRP的相对活性高于游离酶，固定化HRP的最适pH为10，高于游离酶的最适pH值(PH 90)，固定化使酶在较宽的pH范围内保持稳定。固定化HRP的表观动力学常数(K-m)为3784 mmolml(-1)，高于游离HRP的表观动力学常数(K-m)；并可在连续6个周期后保留658%的剩余活性(C)2010爱思唯尔B V。保留所有权利
A method has been developed to immobilize horseradish peroxidase (HRP) on modified chitosan beads by means of graft copolymerization of polyethylacrylate in presence of potassium persulphate and Mohr's salt redox initiator. The activity of free and immobilized HRP was studied FTIR spectroscopy and scanning electron microscopy were used to characterize HRP immobilization. The efficiency of the immobilization was investigated by examining the relative enzymatic activity of free enzyme before and after the HRP immobilization The obtained values were found to each 98.4% The results show that the optimum temperature of immobilized HRP was 45 degrees C. which was identical to that of free enzyme, and the immobilized HRP exhibited a higher relative activity than that of free HRP over 45 degrees C The optimal pH for immobilized HRP was 10, which was higher than that of the free HRP (pH 90), and the immobilization resulted in stabilization of enzyme over a broader pH range. The apparent kinetic constant value (K-m) of immobilized HRP was 3 784 mmol ml(-1), which was higher than that of free HRP On the other hand, the activity of immobilized HRP decreased slowly against time when compared to that of the free HRP. and could retain 65 8% residual activity after 6 consecutive cycles (C) 2010 Elsevier B V. All rights reserved