Mushroom tyrosinase was immobilized by adsorption onto the totally cinnamoylated derivative of D-sorbitol. The polymerization and cross-linking of the derivative initially obtained was achieved by irradiation in the ultraviolet region, where this prepolymer shows maximum sensitivity. Immobilization of tyrosinase on this support involves a process of physical adsorption and intense hydrophobic interactions between the cinnamoyl groups of the support and related groups of the enzyme. The pH value, enzyme concentration and immobilization time were all important parameters affecting immobilization efficiency; also, enzyme immobilization efficiency correlated well with the tyrosinase isoelectric point. The immobilized enzyme showed an optimum measuring pH of 3.5 and greater activity at acid and neutral pH values than the soluble enzyme. The optimal reaction temperature was 35 degrees C and the temperature profile was broader than that of the free enzyme or of the enzyme immobilized on other supports. The apparent Michaelis constant of mushroom tyrosinase immobilized on the SOTCN derivative acting on 4-tert-butylcatechol (TBC) was 0.40 +/- 0.02 mmol dm(-3), which was lower than for the soluble enzyme, suggesting that the affinity of this enzyme for this substrate was greater when immobilized than when in solution. Immobilization stabilized the enzyme and made it less susceptible to activity loss during storage at pH values in the range 4-5.5, and the suicide inactivation of the immobilized tyrosinase was null or negligible in a reaction medium with 4-tert-butylcatechol at a concentration of 0.4 mmol dm(-3). The results show that cinnamic carbohydrate esters of D-sorbitol are an appropriate support for tyrosinase immobilization and could be of use for several tyrosinase applications. (c) 2005 Society of Chemical Industry.