Immobilization of the Peroxygenase from Agrocybe aegerita. The Effect of the Immobilization pH on the Features of an Ionically Exchanged Dimeric Peroxygenase

This paper outlines the immobilization of recombinant dimeric unspecific peroxygenase from Agrocybe aegerita (rAaeUPO). The enzyme was quite stable (remaining unaltered its activity after 35 h at 47 °C and pH 7.0). Phosphate destabilized enzyme, while glycerol stabilized it. not immobilized on glyoxyl-agarose supports, it albeit in inactive form vinyl-sulfone-activated supports. rAaeUPO glutaraldehyde pre-activated supports gave almost quantitative yield retained some activity, but biocatalyst very unstable. Its via anion exchange PEI also produced good yields, stability dropped. However, using aminated agarose, activity. strongly depended pH, being much less when adsorbed 9.0 than 7.0 or 5.0 (residual 0 for former 80% other preparations), presenting similar to that free enzyme. is a clear example how greatly affects final performance.