Tyrosinase has diverse functions in biological systems including melanin synthesis for defense against harmful effects of ultraviolet light. It oxidizes tyrosine especiallyL-3, 4-dihydroxyphenylalanineto L-Dopaquinone. The objective is to isolate, partially purify and immobilize tyrosinase on coconut fiber and palm wood chips using gum Arabic as binder. Yam (Dioscorea rotundata) was used as source of tyrosinase. It was extracted by mashing yam with potassium phosphate buffer (P^H 7). The slurry was centrifuged, supernatant decanted and mixed with solid ammonium sulphate [(NH₄)₂SO₄] for partial purification of the enzyme. Its kinetic parameters were determined spectrophotometrically by measuring its activity at varying concentrations of substrate (L-DOPA). Line weaver-bulk double reciprocal plot was plotted to derive Michealis-Menten constant (K_m) and maximum velocity (V_max) while the optimum temperature and P^H was determined by varying temperature and P^H ranges (5.5-8.5) of reaction system. The immobilized tyrosinase activitywas compared with that of partially purified enzyme. Results showed that, crude enzyme activity was 7.2 micromoles/min, immobilized enzymes activity on coconut fiber was7.7micromoles/min and that on palm wood chip was 11.1micromoles/min. K_m and V_max of partially purified tyrosinase was 33.3mM and 0.016S^-1, that of immobilized enzyme on coconut fiber was 28.5mM and 0.020s^-1 while that on palm wood chips was 20.8mM and 0.033s^-1 respectively. Optimum P^H and temperature for partially purified and immobilized enzymes was 6.5 and 55⁰C. Immobilization of yam tyrosinase on palm wood chips increased the activity of partially purified enzyme by 15%. Conclusively, palm wood chip is considered a better support to coconut fiber for immobilization of yam tyrosinase.