Mediator-assisted laccase-catalyzed oxidation of 4-hydroxybiphenyl |
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Authors: | I. Bratkovskaya R. Ivanec J. Kulys |
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Affiliation: | (1) Institute of Biochemistry, Mokslininku 12, Vilnius, LT-08662, Lithuania;(2) Department of Chemistry and Bioengineering, Vilnius Gediminas Technical University, Sauletekio Av. 11, Vilnius, LT-10223, Lithuania |
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Abstract: | The kinetics of oxidation of 4-hydroxybiphenyl (4-HBP) catalyzed by laccase from Polyporus pinsitus was studied in the presence of methyl syringate (MS), which acts as an electron-transfer mediator. Measurements were performed in 0.05 M acetate buffer, pH 5.5, in the presence of 4-HBP, MS, and laccase. It is shown that the oxidation rate of the lowly reactive substrate 4-HBP significantly increases during synergistic action of the highly reactive substrate MS. Bimolecular kinetic constants of interaction between the oxidized form of laccase and MS, the former and 4-HBP, and the oxidized form of MS and 4-HBP were calculated. A kinetic scheme of the synergistic substrate action is suggested; based on this scheme, the dependence of the initial rate on reagent concentration is derived. Analyzing experimental data, we obtained kinetic constants close to those obtained by modeling the processes. |
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Keywords: | 4-hydroxybiphenyl laccase methyl syringate synergistic mechanism kinetic constants |
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