Bilirubin Removal by the Pseudoperoxidase Activity of Free and Immobilized Hemoglobin and Hemoglobin Co-Immobilized with Glucose Oxidase

We report a process for oxidizing bilirubin. Hemoglobin in the presence of an oxidizing agent can effectively oxidize bilirubin. Hemoglobin can be used either in free form or immobilized. Immobilisation includes microencapsulation, covalent linkage to carriers, intermolecular crosslinking into polyhemoglobin and others. The oxidizing agent can be added in the form of a peroxide. However, no external peroxide is required when hemoglobin is co-immobilized with glucose oxidase. In this case, the oxidation reaction takes place in the presence of glucose which is normally available in the blood stream and the presence of other oxidizing agents becomes unnecessary. In cases where bilirubin is conjugated to large proteins such as albumin, oxidation can be accomplished by using hemoglobin either in free form, adsorbed or bound on a suitable surface. Polyhemoglobin or cross-linked hemoglobins can also be used as oxidation catalysts in this case.