Literature DB >> 16732735

Mediator-assisted laccase-catalyzed oxidation of 4-hydroxybiphenyl.

I Bratkovskaya1, R Ivanec, J Kulys.   

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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Year:  2006        PMID: 16732735     DOI: 10.1134/s0006297906050130

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  2 in total

1.  Modelling of amperometric biosensor used for synergistic substrates determination.

Authors:  Dainius Simelevicius; Romas Baronas; Juozas Kulys
Journal:  Sensors (Basel)       Date:  2012-04-16       Impact factor: 3.576

2.  The TRPA1 agonist, methyl syringate suppresses food intake and gastric emptying.

Authors:  Min Jung Kim; Hee Jin Son; Seo Hyeon Song; Myungji Jung; Yiseul Kim; Mee-Ra Rhyu
Journal:  PLoS One       Date:  2013-08-21       Impact factor: 3.240

  2 in total

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