Immobilization of thermophilic lipase in inorganic hybrid nanoflower through biomimetic mineralization.
Immobilization of thermophilic lipase in inorganic hybrid nanoflower through biomimetic mineralization.
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DOI：
10.1016/j.colsurfb.2020.111450
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发表时间：
2020-11
期刊：
影响因子：
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通讯作者：
Yong Liu;Xinxin Shao;Deqiang Kong;Guangquan Li;Quanshun Li
中科院分区：
文献类型：
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作者：
Yong Liu;Xinxin Shao;Deqiang Kong;Guangquan Li;Quanshun Li
产自Alcaligenessp.通过仿生矿化的方法，成功地将其固定在基于Cu3（PO4）2的无机杂化纳米花中。对固定化酶的形态、结构和元素组成进行了系统的表征，以阐明酶分子的成功负载。通过对辛酸对硝基苯酯水解反应的监测，确定了固定化酶的最适温度（65 ° C）和最适pH（8.0）。此外，与游离酶相比，无机杂交纳米花中的固定化酶对热、pH和金属离子的稳定性增强，这归因于纳米花外壳的保护作用。固定化酶具有良好的重复使用性和长期贮存稳定性，重复使用8次或室温下放置4周后酶活力略有下降。总之，无机杂化纳米花固定化技术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有效的方法，在开发未来生物催化应用的理想催化剂方面显示出巨大的潜力。
Thermophilic lipase QLM fromAlcaligenessp. 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 ofp-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.