Apart from higher stability, immobilization of an enzyme as CLEC also offers the advantage of easy enzyme recovery from a product stream and reuse in biocatalytic reactions. Therefore, repeated batch reactions with cyclohexene oxide (1) and azide at 22°C were performed for each 24 h with daily reuse of D114C CLECs over a total of 21 days. After each reaction, the CLECs were separated by centrifugation before reuse in a new batch reaction. As shown in Figure , D114C CLECs displayed activity over all reaction cycles, obtaining still 87% and 70% of the initially observed conversion after 5 and 21 days, respectively. The observed sligth decrease in enantiomeric excess during this time span can be explained by a stronger influence of the chemical background reaction with decreasing enzyme activity. Microscopic analysis of the D114C CLECs after the 21 reaction cycles confirmed that they retained their hexagonal shape with sizes of about 100 µm (Figure ). In addition to cyclohexene oxide, we also tested the application and reuse of D114C CLECs in the azidolysis of phenylglycidylether (3) , styrene oxide (5) , phenylpropylene oxide (7) and limonene oxide (9) , which had been demonstrated previously to be converted by HheG. Daily reuse of D114C CLECs over 5 cycles yielded no or only a slight decrease in conversion with these four epoxide substrates (Figure ). The activity recovery comparing conversion in the first and fifth cycle was 99.4% (3), 100% (5), 93.9% (7) and 91.1% (9). In comparison, CLEAs of HheC from Agrobacterium radiobacter AD1 displayed an activity recovery of 74% after 10 reaction cycles of each 30 min in the conversion of 5 mM 1,3-dichloro-2-propanol. Hence, our data demonstrate the effectiveness of HheG immobilization via CLEC formation to obtain a stable and reusable biocatalyst.