Akademik Veri Yönetim Sistemi
FRESENIUS ENVIRONMENTAL BULLETIN, cilt.27, sa.7, ss.4844-4856, 2018 (SCI-Expanded)
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°C to 30°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