Immobilization of enzymes through metal-based system is demonstrated as a promising approach to enhance its properties. In this study, the influence of metals ions, including copper, cobalt and zinc (Zn) on the immobilization of β-glucosidase (BGL) through the synthesis of protein-inorganic hybrid was evaluated at 4 °C. Among these metal ions-based hybrids, Zn showed the highest encapsulation yield and relative activity of 87.5 and 207%, respectively. Immobilized BGL exhibited higher pH and temperature stability compared to free form. Thermal stability of hybrid improved up to 26-fold at 60 °C. After 10 cycles of reuse, immobilized enzyme retained 93.8% of residual activity. These results suggested that metal ions played a significant role in the enzyme immobilization as a protein-inorganic hybrid. Overall, this strategy can be potentially applied to enhance the properties of enzymes though effective encapsulation for the broad biotechnological applications.

中文翻译：

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金属离子对通过蛋白质-无机杂种固定化β-葡萄糖苷酶的影响。

通过基于金属的系统固定酶被证明是增强其性能的一种有前途的方法。在这项研究中，在4°C下评估了包括铜，钴和锌（Zn）在内的金属离子对通过蛋白质-无机杂化剂的合成固定化β-葡萄糖苷酶（BGL）的影响。在这些基于金属离子的杂化物中，Zn的包封率最高，相对活性分别为87.5和207％。与游离形式相比，固定化的BGL具有更高的pH和温度稳定性。在60°C下，杂种的热稳定性提高了26倍。在重复使用10个循环后，固定化酶保留了93.8％的残留活性。这些结果表明，金属离子作为蛋白质-无机杂化体在固定化酶中起着重要作用。总体，