High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase.

The H(2)O(2) supply strategy was one of crucial factors for high efficient degradation of pollutants with lignin peroxidase (LiP). In this paper, an attempt was made to couple a H(2)O(2) producing enzymatic reaction to the LiP catalyzed oxidation of dyes. H(2)O(2) needed was generated by glucose oxidase (GOD) and its substrate glucose. The generation rate of H(2)O(2) could be easily controlled by adjusting the pH of the degradation system and the amount of GOD added. Due to the controlled release of H(2)O(2), a sustainable constant activity of LiP was observed. The inhibition of LiP by high level H(2)O(2) supplied externally by a single addition at the beginning of the experiments could be avoided. Degradation of three dyes (xylene cyanol, fuchsine and rhodamine B) with LiP coupled with GOD indicated that the present H(2)O(2) supply strategy was very effective for improvement of the efficiency of the decolourization of dyes.