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首页> 外文期刊>Catalysts >Preparation of Cross-Linked Glucoamylase Aggregates Immobilization by Using Dextrin and Xanthan Gum as Protecting Agents
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Preparation of Cross-Linked Glucoamylase Aggregates Immobilization by Using Dextrin and Xanthan Gum as Protecting Agents

机译：用糊精和黄原胶作为保护剂制备交联的葡糖淀粉酶骨料

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摘要

In this paper glucoamylase from Aspergillus niger was immobilized by using a modified version of cross-linked enzyme aggregates (CLEA). The co-aggregates were cross-linked with glutaraldehyde; meanwhile dextrin and xanthan gum as protecting agents were added, which provides high affinity with the enzyme molecules. The immobilized glucoamylase was stable over a broad range of pH (3.0–8.0) and temperature (55–75 °C); dependence shows more catalytic activity than a free enzyme. The thermostability, kinetic behavior, and first-order inactivation rate constant ( k i ) were investigated. The two types of protector made the immobilized glucoamylase more robust than the free form. Both of the immobilized enzymes have excellent recyclability, retaining over 45% of the relative activity after 24 runs. In addition, immobilized enzymes reduced only 40% of the initial activity after three months by the storability measure, indicating high activity.
机译：在本文中，使用改良版的交联酶聚集体（CLEA）固定了黑曲霉的葡糖淀粉酶。共聚集体与戊二醛交联;同时加入糊精和黄原胶作为保护剂，与酶分子具有很高的亲和力。固定的葡糖淀粉酶在广泛的pH（3.0–8.0）和温度（55–75°C）范围内稳定;依赖性显示比游离酶更多的催化活性。研究了热稳定性，动力学行为和一阶失活速率常数（k i）。两种类型的保护剂使固定的葡糖淀粉酶比游离形式更坚固。两种固定化酶都具有出色的可回收性，在24次运行后保留了超过45％的相对活性。此外，固定性酶在3个月后的耐贮存性仅降低了其初始活性的40％，表明其活性较高。

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