Poly(2‐oxazoline)s with a 2,2′‐Iminodiacetate End Group Inhibit and Stabilize Laccase

Poly(2‐oxazoline)s (POxs) with 2,2′‐iminodiacetate (IDA) end groups were investigated as inhibitors for laccase. The polymers with the IDA end groups are reversible, competitive inhibitors for this enzyme. The IC50 values were found to be in a range of 1–3 mm. Compared with IDA alone, the activity was increased by a factor of more than 30; thus indicating that attaching a polymer chain to an inhibitor can already improve the activity of the former. The enzyme activity drops to practically zero upon increasing the concentration of the most active telechelic inhibitor, IDA‐PEtOx30‐IDA (PEtOx: poly(2‐ethyl‐2‐oxazoline)), from 5 to 8 mm. This unusual behavior was investigated by means of dynamic light scattering, which showed specific aggregation above 5 mm. Furthermore, the laccase could be stabilized in the presence of POx‐IDA, upon addition at a concentration of 20 mm and higher. Whereas laccase becomes completely inactive at room temperature after one week, the stabilized laccase is fully active for at least a month in aqueous solution.
Bulking up: Poly(2‐oxazoline)s (POx) with iminodiacetate (IDA) end groups competitively inhibit the enzyme laccase. A telechelic IDA‐POx‐IDA derivative shifts the inhibition mechanism at higher concentrations to become a dead‐end inhibitor. Simultaneously, the polymers stabilize the enzyme to preserve its activity, even for 28 days at room temperature.