Co-immobilization of oxalate oxidase and catalase in films for scavenging of oxygen or oxalic acid

Oxalate oxidase has potential to act as an oxygen scavenger in active packaging to increase the shelf-life of food and beverages, while simultaneously producing the protective packaging gas carbon dioxide. This study shows that oxalate oxidase from barley can be immobilized with retained catalytic activity through entrapment in a latex polymer matrix. Conditions for formation of film containing oxalate oxidase have been evaluated as well as effects of storage and latex on enzyme activity, migration of enzyme in films, and the ability of the latex films to resist higher temperatures. Drying of enzyme-containing latex films at 75 °C prior to conditioning at 30 °C resulted in higher activity than drying solely at 30 °C, or drying at 95 °C or 105 °C followed by conditioning at 30 °C. Storage of films in air at 4 °C for 14 days did not negatively affect the enzymatic activity. Inclusion of catalase in films with oxalate oxidase effectively prevented release of hydrogen peroxide. The results suggest that the immobilized enzyme can successfully be used both as an oxygen scavenger and as an oxalic-acid scavenger.

► Highlights ► Oxalate oxidase and catalase were co-immobilized by entrapment. ► Immobilized oxalate oxidase can act as an oxygen or oxalic acid scavenger. ► Catalase prevented release of hydrogen peroxide from films with oxalate oxidase.