Immobilized onion leaves tyrosinase on agar-Abelmoschus esculentus

To revaluates the catalytic mechanism of onion leaves tyrosinase and its behavioral study were performed by immobilized it in agar-Abelmoschus esculentus polymer. Soluble and immobilized tyrosinase exhibited Km 5μM and 8.33μM; Vmax 167μmol/lit/min and 90μmol/lit/min; optimum pH 7.2; Optimum pH 7.0, Optimum temperature 50°C and 60°C, Ea 108.35 Kcal/mol and 78.80 Kcal/mol respectively. Immobilized tyrosinase was more heat stable and longer stability than soluble tyrosinase. Immobilized activity maxima investigated at 35 min having storage stability 75–80% while 65% for soluble. Nevertheless, soluble tyrosinase had higher affinity for the substrate as compared to immobilize. Concluding, agar: Abelmoschus esculentus composite matrix provides natural ambient to enzyme; may be utilized for industrial purpose.