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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Modification and characterization of cellulosic cotton fibers for efficient immobilization of urease
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Modification and characterization of cellulosic cotton fibers for efficient immobilization of urease

机译:纤维素棉纤维的改性和表征,可有效固定尿素酶

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Cotton fibers were first grafted by polyacrylonitril in the presence of KMnO _4 and oxalic acid as a combined redox initiator. Moreover, modification of the grafted cotton fibers was done by changing the nitrile group (CN) into hydrazidine group through the reaction with hydrazine hydrate, then the fibers were activated by glutaraldehyde to introduce free aldehyde groups which were able to react with amino groups of urease to form Schiff's base, and result in cotton fibers immobilized urease. The efficiency of the immobilization was evaluated by examining the relative enzymatic activity of enzyme before and after the immobilization of urease. The results showed that the optimum temperature of immobilized urease was 35°C, which was higher than that of the free enzyme (30°C), and the immobilized urease exhibited a higher relative activity than that of free urease over 35°C. The optimal pH for immobilized urease was 6.5, which was lower than that of the free urease (pH 7.0), and the immobilization resulted in stabilization of enzyme over a wider pH range. The kinetic constant value (K _m) of immobilized urease was higher than that of the free urease. However, the thermal and operational stabilities of immobilized urease have been improved greatly.
机译:首先在KMnO_4和草酸作为氧化还原引发剂的存在下,将聚丙烯腈接枝棉纤维。此外,接枝棉纤维的改性是通过与水合肼反应将腈基(CN)转变为肼基,然后用戊二醛将纤维活化而引入能够与脲酶的氨基反应的游离醛基。形成席夫氏碱,并导致棉纤维固定化脲酶。通过检查脲酶固定之前和之后酶的相对酶活性来评估固定效率。结果表明,固定化脲酶的最适温度为35℃,高于游离酶的最佳温度(30℃),固定化脲酶在35℃以上的相对活性高于游离脲酶。固定尿素酶的最佳pH为6.5,低于游离脲酶的最佳pH(pH 7.0),并且固定导致酶在较宽的pH范围内稳定。固定化脲酶的动力学常数(K_m)高于游离脲酶的动力学常数。但是,固定化脲酶的热稳定性和操作稳定性已大大提高。

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