A biocompatible support made of ZnGlu‐coated magnetic iron oxide nanoparticles (ZnGlu–MNPs) was prepared by a simple electrostatic self‐assembly technique and structurally characterized. Aspergillus niger lipase (ANL) was immobilized onto the ZnGlu–MNPs with high protein loading (118.0 mg g−1) and high enzyme‐activity recovery (more than 82.0 %). The as‐prepared immobilized ANL exhibits high catalytic performance and a wide pH and temperature adaptability. Moreover, the stabilities and the solvent tolerance of ANL@ZnGlu‐MNPs were clearly superior to those of the free counterpart. The novel ANL@ZnGlu‐MNPs was easily recycled from the reaction medium by magnetic forces. Therefore, the as‐prepared ZnGlu‐MNPs is a promising novel carrier for immobilized enzymes.

A newly immobilized Aspergillus niger lipase (ANL@ZnGlu-MNPs) was employed for the preparation of 1,2-epoxycyclooctane by oxidation of cyclooctene. The chosen variables, including substrate concentration, reaction temperature, immobilized enzyme dose, and H2O2 dose, were optimized in the reaction system of ethyl acetate. The yield and the enantiomeric excess of the product were achieved at 56.8% and 84.1%, respectively, under the following optimum reaction conditions: the concentration of substrate (cyclooctene) was 150 mM, the dosages of immobilized enzyme (ANL@ZnGlu-MNPs) and hydrogen peroxide were respectively 100 mg and 4.4 mmol, and the reaction was carried out in the system of 4 mL ethyl acetate at 40 °C. Further study on the operational stability of ANL@ZnGlu-MNPs showed that more than 51.6% of product yield was obtained after reusing for ten batches. A novel immobilized lipase was prepared and applied to synthesize 1,2-epoxycyclooctane from cyclooctene. Although ANL@ZnGlu-MNPs performs well in operational stability and the reaction can achieve high enantiomeric purity of the product, the yield of the catalytic reaction needs to be further improved.

The Cover shows a novel biocompatible enzyme carrier consisting of ZnGlu‐coated magnetic iron oxide nanoparticles (ZnGlu–MNPs), which were prepared by a simple electrostatic‐self‐assembly technique.In their Full Paper, G.‐H. Xia, S.‐L. Cao et al. describe the structural characterization of ZnGlu–MNPs and their use as enzyme carrier for the immobilization of Aspergillus niger lipase. The as‐prepared nanobiocatalyst (ANL@ZnGlu–MNPs) exhibited high catalytic performance, which is significantly superior to that of its free counterpart. The catalyst was easily recovered from the reaction medium by magnetic forces. Therefore, ZnGlu–MNPs are promising novel carriers for enzyme immobilization. More information can be found in the Full Paper by G.‐H. Xia, S.‐L. Cao et al. on page 1794 in Issue 10, 2017 (DOI: 10.1002/cctc.201700070).