Oxygen scavengers are used in active packages to protect the food against deteriorative oxidation processes. The aim of this work was to investigate the possibilities to produce oxygen-scavenging packaging materials based on oxygen-reducing enzymes. The enzymes were incorporated into a dispersion coating formulation applied onto a food-packaging board using conventional laboratory coating techniques. Various enzymes were used: a glucose oxidase, an oxalate oxidase and three laccases originating from different organisms. All of the enzymes were successfully incorporated into a coating layer and could be reactivated after drying. For at least two of the enzymes, re-activation was possible not only by using liquid water but also by using water vapour. Re-activation of the glucose oxidase and a laccase required relative humidities of greater than 75% and greater than 92%, respectively. Catalytic reduction of oxygen gas by glucose oxidase was promoted by creating an open structure through addition of clay to the coating at a level above the critical pigment volume concentration. Migration of the enzyme and the substrate was reduced by adding an extrusion-coated liner of polypropylene on top of the coating. For the laccase-catalysed reduction of oxygen it was possible to use lignin derivatives as substrates for the enzymatic reaction. The laccase-catalysed reaction created a polymeric network by cross-linking of lignin-based entities, which resulted in increased stiffness and increased water-resistance of biopolymer films. The laccases were also investigated with regard to their potential to function as oxygen scavengers at low temperatures. At 7°C all three laccases retained more than 20% of the activity they had at room temperature (25°C), which suggests that the system is also useful for packaging of refrigerated food.