首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Immobilization of alpha-amylase on chitosan-montmorillonite nanocomposite beads
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Immobilization of alpha-amylase on chitosan-montmorillonite nanocomposite beads

机译:在壳聚糖 - 蒙脱石纳米复合材料珠粒上固定α-淀粉酶

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摘要

Enzyme immobilization is a way to increase efficiency of the enzyme and facilitate its recovery. The aim of this study was to immobilize alpha-amylase on chitosan-montmorillonite nanocomposite beads. Nanocomposite beads were prepared as the carrier for the enzyme stabilization and their surface was modified by Glutaraldehyde. Alpha-amylase was immobilized on nanocomposite beads by covalent bonding. The results of scanning electron microscopy (SEM) showed that particle size range of montmorillonite was 10-30 nm. This study indicated that the enzyme immobilization efficiency was 87%. The activity of free and immobilized enzyme during 40 days of storage at 4 degrees C decreased 95% and 36%, respectively. The results showed that the immobilized enzyme activity after reusing five times decreased about 47%. This study indicated that the immobilized enzyme activity was higher than the free enzyme at different temperatures. Also the immobilized enzyme was more stable than the free enzyme at lower pH. The results of kinetic parameters showed that K-m values of the immobilized enzyme (9.12 mu mol/m1) were higher than free enzyme (6.80 mu mol/ml). The V-max values for the free and immobilized enzyme were 130 and 0.629) mu mol/mg.min, respectively. (C) 2018 Published by Elsevier B.V.
机译:酶固定化是提高酶效率并促进其恢复的方法。本研究的目的是将α-淀粉酶固定在壳聚糖 - 蒙脱石纳米复合材料珠粒上。制备纳米复合珠作为酶稳定化的载体,并通过戊二醛改性它们的表面。通过共价键合将α-淀粉酶固定在纳米复合珠上。扫描电子显微镜(SEM)的结果表明,蒙脱石的粒度范围为10-30nm。本研究表明,酶固定效率为87%。在4℃下40天储存期间的自由和固定化酶的活性分别降低了95%和36%。结果表明,重用五次后固定的酶活性降低约47%。该研究表明,固定化的酶活性高于不同温度下的游离酶。此外,固定化的酶比在较低pH下的游离酶更稳定。动力学参数的结果表明,固定化酶的K-M值(9.12μmol/ m1)高于游离酶(6.80μmmol/ ml)。自由和固定化酶的V-Max值分别为130和0.629)mu mol / mg.min。 (c)2018由elestvier b.v出版。

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