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Abstract
The hepatic microsomal UDP-Glucuronyl transferase which catalyze the glucuronidation of drugs, pesticides, carcinogens and other xenobiotics, was immobilized by entrappment in chitosan. Chemical and physical characterization were made by using 1-naphthol as substrate. Thermal, storage and operational stabilities of the immobilized enzyme was also searched and found to be better in comparison with the free enzyme. In conclusion, chitosan gel beads appear to have good characteristics for use as UDPGT immobilization support suitable for large scale use and offer the prospect that immobilized UDPGT may become an important form of catalyst in medicine.