Immobilization of polyphenol oxidase enzyme on new matrix antimony doped tin oxide (SnO2:Sb) thin film

Abstract

Polyphenol oxidase enzymes (PPOs) obtained from Agseftali (Prunus persica L.), which was native peach genotypes under Igdir province ecological condition in Turkey, was purified by affinity chromatography and then, PPOs immobilized on new matrix antimony doped tin oxide (SnO2:Sb) thin films by adsorption method for the first time. in here, the films were synthesized by spray pyrolysis technique in laboratory condition, easily. the immobilization of PPOs onto SnO2:Sb thin films was confirmed by scanning electron microscopy (SEM) and fourier transform infrared spectroscopy (FTIR). Obtained free and immobilized PPOs onto thin film were compared according to some enzyme optimization points such as optimum pH and temperature. the optimum pH of the free and immobilized PPOs was found as 6.0. the optimum temperature of PPOs increased from 20 degrees C to 30 degrees C with immobilization on the thin film. Km values of the free and immobilized enzymes were obtained as 2 mM and 1.4 mM, respectively. L-Tyrosine oxidation of the enzymes enhanced with immobilization of PPOs onto SnO2:Sb thin films. the immobilization on SnO2:Sb thin films aslo provided to increase the satibilty and life time of the PPOs because they could be used 3 times and retained approximately 50% of activity following 18 repeated usage in a 15 days. the PPOs can be thougt as an activist towards 4-methylcatechol substrate and, the usability of the enzymes can be significantly increased via immobilization onto SnO2:Sb thin films.