Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China.
Jilin Provincial Key Laboratory on Molecular and Chemical Genetics, The Second Hospital of Jilin University, Changchun 130012, China.
Colloids Surf B Biointerfaces. 2021 Jan;197:111450. doi: 10.1016/j.colsurfb.2020.111450. Epub 2020 Nov 6.
Thermophilic lipase QLM from Alcaligenes sp. was successfully immobilized in Cu(PO)-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.
嗜热脂肪酶 QLM 来源于产碱杆菌，通过仿生矿化成功固定在基于 Cu(PO)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。通过监测对硝基苯辛酸酯的水解，确定了固定化酶的最佳温度（65°C）和 pH（8.0）。此外，与游离酶相比，固定在无机杂化纳米花中的酶在热、pH 和金属离子方面表现出增强的稳定性，这归因于纳米花壳的保护作用。此外，固定化酶具有良好的可重复使用性和长期储存稳定性，在重复使用 8 次或在室温下储存在水中 4 周后，其活性略有下降。总的来说，在无机杂化纳米花中的固定化提供了一种简便有效的方法来制备具有良好活性、稳定性和可重复使用性的固定化酶，因此该策略在开发未来生物催化应用中的理想催化剂方面显示出巨大的潜力。
