Substrate-dependent kinetics in tyrosinase-based biosensing: amperometry vs. spectrophotometry
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چکیده
منابع مشابه
Substrate-dependent kinetics in tyrosinase-based biosensing: amperometry vs. spectrophotometry.
Despite the broad use of enzymes in electroanalytical biosensors, the influence of enzyme kinetics on the function of prototype sensors is often overlooked or neglected. In the present study, we employ amperometry as an alternative or complementary method to study the kinetics of tyrosinase, whose catalytic activity results in o-quinone products. We further compare our results for four monophen...
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Biodegradation of phenol in the presence of glucose as a supplementary substrate was investigated with mixed microbial consortium isolated from waste effluent of coke-steel factory. Batch experiments were carried out at room temperature and pH value of 7. Initial phenol and glucose concentrations were in the range of 25-1000 mg/l and 500-3000 mg/l, respectively. In a dual substrates system the ...
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An amperometric biosensor was constructed by using ZnO nanorod clusters as platforms for immobilizing tyrosinase on the nanocrystalline diamond (NCD) electrodes. The results showed that ZnO nanorod clusters provided an advantageous microenvironment due to their favorable isoelectric point (IEP) for tyrosinase loading; immobilized tyrosinase generally retained its activity. The tyrosinase/ZnO/NC...
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Anisic acid (p-methoxybenzoic acid) was characterized as a tyrosinase inhibitor from ani-seed, a common food spice. It inhibited the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) catalyzed by tyrosinase with an IC50 of 0.60 mM. The inhibition of tyrosinase by anisic acid is a reversible reaction with residual enzyme activity. This phenolic acid was found to be a classical noncompetitive in...
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ژورنال
عنوان ژورنال: Analytical and Bioanalytical Chemistry
سال: 2012
ISSN: 1618-2642,1618-2650
DOI: 10.1007/s00216-012-5964-0