Immobilization of tyrosinase in polysiloxane/polypyrrole copolymer matrices

Abstract

Immobilization of tyrosinase in conducting copolymer matrices of pyrrole functionalized polydimethylsiloxane/polypyrrole (PDMS/PPy) was achieved by electrochemical polymerization. The polysiloxane/polypyrrole/tyrosinase electrode was constructed by the entrapment of enzyme in conducting matrices during electrochemical copolymerization. Maximum reaction rate (V(max)) and Michaelis-Menten constant (K(m)) were investigated for immobilized enzyme. Enzyme electrodes were prepared in two different electrolyte/solvent systems. The effect of supporting electrolytes, p-toluene sulfonic acid and sodium dodecyl sulfate on the enzyme activity and film morphology were determined. Temperature and pH optimization, operational stability and shelf-life of enzyme electrodes were also examined. Phenolic contents of green and black tea were determined by using enzyme electrodes.

Various applications of immobilized glucose oxidase and polyphenol oxidase in a conducting polymer matrix

“…Then, o-dihydroxybenzenes are oxidized to o-quinones which is called as catecholase activity. Polyphenol biosenors were constructed in order to determine phenolic concentration in tea [7], red wine [8,9] and remove phenol from wastewater [10].…”

Electrode Materials (Bulk Materials and Modification)

“…[506][507][508] One of the most common example is the use of tyrosinase (also known as polyphenol oxidase) for the detection of phenol derivatives. [560][561][562][563][564][565] The enzyme can be immobilized in a polypyrrole or polyaniline matrix by either entrapment, covalent attachment or biotin-avidin interactions. Limits of detection between 10 nM and 1 μM have been reached by amperometry.…”

Layer-by-Layer coated tyrosinase: An efficient and selective synthesis of catechols

“…The influence of pH on the immobilization procedure was also studied in the range of 5.0-8.0. The optimum binding was achieved with sodium phosphate buffer at pH 7.0 (Table 1 entries 5 vs [7][8][9]. With the aim to further increase the stability of Tyro/E, the LbL technique was applied by coating Tyro/E through a sequential deposition of charged polyelectrolytes.…”

“…6 Moreover, the possibility to immobilize tyrosinase on stable and low cost supports further increase the interest for this enzyme in industrial applications. 7 Examples of the immobilization of tyrosinase on carbon nanotube, 8 copolymer matrices, 9 chitosan, 10 gold nanoparticles, 11 alumina sol-gel, 12 membrane alginate, polyacrylamide, and gelatine gels 13 have been reported in the production of L-dopa, 14 in the removal of phenolic compounds from waste water, 15 and in other industrial applications. 16 However, some of these immobilization methods are rather complicated and do not give good enzyme stability or retention.…”