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首页> 外文期刊>Acta microbiologica et immunologica Hungarica: A quarterly of the Hungarian Academy of Sciences >Immobilization of polygalacturonase from Aspergillus niger onto activated polyethylene and its application in apple juice clarification.
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Immobilization of polygalacturonase from Aspergillus niger onto activated polyethylene and its application in apple juice clarification.

机译：将黑曲霉中的聚半乳糖醛酸酶固定在活化的聚乙烯上，并将其用于澄清苹果汁中。

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摘要

The present work is focused on efficient immobilization of polygalacturonase on polyethylene matrix, followed by its application in apple juice clarification. Immobilization of polygalacturonase on activated polyethylene and its use in apple juice clarification was not reported so far. Aspergillus niger Van Tieghem (MTCC 3323) produced polygalacturonase when grown in modified Riviere's medium containing pectin as single carbon source by fed-batch culture. The enzyme was precipitated with ethanol and purified by gel filtration chromatography (Sephacryl S-100) and immobilized onto glutaraldehyde-activated polyethylene. The method is very simple and time saving for enzyme immobilization. Various characteristics of immobilized enzyme such as optimum reaction temperature and pH, temperature and pH stability, binding kinetics, efficiency of binding, reusability and metal ion effect on immobilized enzymes were evaluated in comparison to the free enzyme. Both the free and immobilized enzyme showed maximum activity at a temperature of 45 degrees C and pH 4.8. Maximum binding efficiency was 38%. The immobilized enzyme was reusable for 3 cycles with 50% loss of activity after the third cycle. Twenty-four U of immobilized enzyme at 45 degrees C and 1 h incubation time increased the transmittance of the apple juice by about 55% at 650 nm. The immobilized enzyme can be of industrial advantage in terms of sturdiness, availability, inertness, low price, reusability and temperature stability.
机译：目前的工作集中在聚半乳糖醛酸酶在聚乙烯基质上的有效固定，随后在苹果汁澄清中的应用。到目前为止，尚未报道聚半乳糖醛酸酶在活化聚乙烯上的固定及其在苹果汁澄清中的用途。当黑曲霉Van Tieghem（MTCC 3323）通过分批补料分批培养在含有果胶作为单一碳源的改良Riviere培养基中生长时，产生了半乳糖醛酸酶。用乙醇沉淀该酶，并通过凝胶过滤色谱法（Sephacryl S-100）纯化，并固定在戊二醛活化的聚乙烯上。该方法非常简单并且节省了酶固定的时间。与游离酶相比，评估了固定化酶的各种特性，例如最佳反应温度和pH，温度和pH稳定性，结合动力学，结合效率，重用性和金属离子对固定化酶的影响。游离酶和固定化酶在45摄氏度和pH 4.8下均显示出最大活性。最大结合效率为38％。固定的酶可重复使用3个循环，第三个循环后活性降低50％。在45摄氏度和1小时的孵育时间下，二十四个固定化酶将苹果汁在650 nm处的透射率提高了约55％。固定的酶在坚固性，可用性，惰性，低价，可重复使用性和温度稳定性方面可以具有工业优势。

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