| dc.description.abstract | Tyrosinase is a copper-containing oxidase, which catalyzes the first 2 steps in mammalian melanogenesis and responsible for enzymatic browning reactions. This study aims to develop and characterize tyrosinase biosensor of zeolite composite and its stability. The enzyme should be properly attached to the transducer for maintaining enzyme activity. Tyrosinase activity was monitored by L-DOPA as a substrate. The optimum conditions of tyrosinase activity obtained by respon optimizer were tyrosinase 50 U/mL and zeolite 150 mg/mL. Using of ferrocene as mediator and zeolite as the immobilization matrix on electrode increased the activity of tyrosinase. KMapp and Imaks app values of tyrosinase were determined by Lineweaver-Burk method, giving 6.04 mM and 6.42 mM, respectively. The electrode of zeolite as immobilizing matrix was relatively stable until 2 hours, the remaining tyrosinase activity was 87.45% | en |
