The hydrolysis of phenolic compounds using an immobilized and highly active and stable derivative of
laccase from Trametes versicolor is presented. The enzyme was immobilized on aldehyde supports. For
this, the enzyme was enriched in amino groups by chemical modification of its carboxyl groups. The
aminated enzyme was immobilized with a high recovered activity (over 60%). Aldehyde derivatives were
more stable than soluble or aminated-soluble enzyme and the reference derivatives after incubation in
different inactivating conditions (high temperatures, different pH values or presence of organic cosolvents).
The most stable derivative was obtained immobilizing the chemically aminated enzyme at pH
10 on aldehyde supports with a stabilization factor approximately 280 fold after incubation at pH 7 and
55 ◦C. In addition, it was possible to prepare immobilized derivatives with a maximal enzyme loading of
60 mg g−1 of support. This derivative could be reused for 10 reaction cycles with negligible lost of activity.