The catalytic properties and stability of soluble and immobilised in nylon-6,6 mesh tyrosinase were studied with the help of an oxygen sensor. A variety of methods were examined for the immobilisation of tyrosinase, although active immobilised enzyme was obtained only with the help of benzidine and dicyclohexylcarbodiimide. The immobilisation caused an increase in the Kmvalue for catechol almost 2 times in comparison with that found for soluble enzyme (0.39 and 0.22 mM, respectively). The immobilised tyrosinase retained sufficient activity for several months. Due to its characteristic suicide inactivation induced by catechol, it is only of single use for analytical purposes.