Thermophilic lipase QLM from Alcaligenes sp. was successfully immobilized in Cu₃(PO₄)₂-based inorganic hybrid nanoflower through biomimetic mineralization. The morphology, structure and element composition of immobilized enzyme were systemically characterized to elucidate the successful loading of enzyme molecules. The optimal temperature (65 °C) and pH (8.0) of immobilized enzyme were then determined by monitoring the hydrolysis of p-nitrophenyl caprylate. Moreover, compared with free enzyme, immobilized enzyme in inorganic hybrid nanoflower exhibited enhanced stability against thermal, pH and metal ions, attributing to the protective effect of nanoflower shell. Additionally, the immobilized enzyme possessed excellent reusability and long-term storage stability, with slightly decreased activity after being repeatedly used for 8 cycles or stored in water at room temperature for 4 weeks. Overall, the immobilization in inorganic hybrid nanoflower provided a facile and effective approach for the preparation of immobilized enzymes with favorable activity, stability and reusability, and thus the strategy showed great potential in developing ideal catalysts for future biocatalytic applications.

来自Alcaligenes sp。的嗜热脂肪酶QLM 。通过仿生矿化成功地将其固定在基于Cu ₃（PO ₄）₂的无机杂化纳米花中。系统地表征了固定化酶的形态，结构和元素组成，以阐明酶分子的成功负载。然后通过监测p的水解来确定固定化酶的最佳温度（65°C）和pH（8.0）-辛基硝基苯酯。此外，与游离酶相比，固定化酶在无机杂种纳米花中表现出对热，pH和金属离子的增强的稳定性，归因于纳米花壳的保护作用。此外，固定化酶具有极好的可重复使用性和长期储存稳定性，在重复使用8个循环或在室温下于水中储存4周后，其活性略有下降。总体而言，无机杂化纳米花中的固定化为制备具有良好活性，稳定性和可重复使用性的固定化酶提供了一种简便而有效的方法，因此该策略显示了开发用于未来生物催化应用的理想催化剂的巨大潜力。