The feasibility of enzyme immobilization into PEG-albumin hydrogels is demonstrated with acid phosphatase and asparaginase. After immobilization, the apparent Km of acid phosphatase was increased by about 11 times when compared with the soluble enzyme. To the contrary, the apparent Km of asparaginase dramatically increased by 150 times, after immobilization. A denaturing effect of the hydrogel swelling on the enzyme activity is hypothesised. For both enzymes, the operational stability at 37 °C was markedly improved by immobilization into the PEG-albumin hydrogels. The in vitro biodegradability of these hydrogels is also demonstrated through protease digestion.Enzymes have long been used in the biomedical field as diagnostic tools or disease markers (1). In the last decade however, they have found new applications as therapeutic agents (2-3). The therapeutic action of an enzyme consists mainly in degrading a substance which is toxic for the organism, due to a pathologic accumulation, an inherited deficiency or an intoxication. A list of enzymes already involved or potentially useful in therapy has been published recently (4). There are various domains of application such as replacement therapy (5-6), spécifie detoxification, scavengers (7), antineoplastic agents (8-11), and prevention of clot formation. Even though there were numerous possibilities of enzyme therapy, two major problems were rapidly identified