Immobilization of paraoxonase onto chitosan and its characterization.

Utku Colak, Nahit Gençer
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引用次数: 10

Abstract

Paraoxonase was covalently immobilized onto a glutaraldehyde containing amino group functionalized chitosan surface by chemical immobilization at pH 8.0. The amount of covalently bound hPON1 was found to be 32 mg/10 chitosan beads. The properties of immobilized enzyme were investigated and compared to those of free enzyme. The effects of various parameters such as pH, temperature, heat, and storage stability on immobilized enzyme were investigated. Kinetic parameters of the immobilized enzyme were also evaluated. Thermal and storage stability experiments were carried out. It was observed that the immobilized enzyme had longer storage stability and retained 50 % of its initial activity during 26 days.

壳聚糖对氧磷酶的固定化及其表征。
在pH 8.0的条件下,用化学固定法将对氧磷酶共价固定在含戊二醛的氨基功能化壳聚糖表面。共价结合hPON1的量为32 mg/10壳聚糖珠。研究了固定化酶的性质,并与游离酶进行了比较。考察了pH、温度、热量、贮存稳定性等参数对固定化酶的影响。并对固定化酶的动力学参数进行了评价。进行了热稳定性和贮存稳定性实验。结果表明,固定化酶具有较长的储存稳定性,在26 d内保持了50%的初始活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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