Residual activity of rAaeUPO on ReliZyme (HA403M, EA403 M) and Purolite (ECR8309F and ECR8285) beads after 40 min plasma-driven biocatalysis. After biocatalysis, enzyme-loaded beads were recovered and washed thrice with potassium phosphate buffer (100 mM, pH 7). Enzyme activity was determined using 2.5 mM 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), 1 mM H2O2 and 50 mM citrate. Samples were shaken during turnover to ensure sufficient substrate supply. Every two minutes in a total of ten minutes reaction time, aliquots of 100 μl were withdrawn and measured at 405 nm using a microplate reader (Biotek Epoch). Enzyme activity was calculated based on the linear slope of the kinetic. Means and standard deviations represent three experiments.