Laccase-catalysed iodide oxidation in presence of methyl syringate

Juozas Kulys1, Irina Bratkovskaja, Regina Vidziunaite

  • 1Department of Enzyme Chemistry, Institute of Biochemistry, Mokslininku 12, LT-08662 Vilnius, Lithuania. jkulys@bchi.lt

Insights

Fungal laccases catalyze potassium triiodide (KI(3)) formation using methyl syringate (MS) as a mediator. Reaction rates vary with laccase type and pH, influenced by redox potential and reversible reaction steps.

Area of Science:

  • Biocatalysis
  • Enzyme kinetics
  • Environmental chemistry

Background:

  • Fungal laccases are versatile oxidoreductases with potential applications in various industrial processes.
  • Understanding the kinetics of laccase-mediated reactions is crucial for optimizing their use.
  • Potassium triiodide (KI(3)) formation is a relevant reaction pathway involving iodide oxidation.

Purpose of the Study:

  • To investigate the kinetics of potassium triiodide (KI(3)) formation catalyzed by fungal laccases.
  • To elucidate the reaction mechanism involving methyl syringate (MS) as a mediator.
  • To compare the activity and kinetic parameters of different recombinant fungal laccase forms.

Main Methods:

  • Utilized recombinant fungal laccase forms: Polyporus pinsitus (rPpL), Myceliophthora thermophila (rMtL), Coprinus cinereus (rCcL), and Rhizoctonia solani (rRsL).
  • Measured triiodide formation rates spectrophotometrically under varying pH conditions (4.5-6.5) and substrate concentrations.
  • Analyzed kinetic data to determine reaction rates, turnover numbers, and reversibility of the catalytic cycle.

Main Results:

  • Triiodide formation rates varied significantly among laccases, with rPpL, rCcL, and rRsL showing higher rates than rMtL at pH 5.5.
  • The reaction rate increased as pH decreased from 6.5 to 4.5.
  • A reaction mechanism was proposed involving methyl syringate oxidation and subsequent reaction with iodide, with reversibility influenced by the laccase's redox potential.

Conclusions:

  • Fungal laccases, particularly rPpL, rCcL, and rRsL, efficiently catalyze KI(3) formation with MS as a mediator.
  • pH significantly impacts the reaction rate, with optimal activity observed at lower pH values.
  • The reversibility of the laccase-mediator interaction plays a key role in the observed kinetic differences and saturation rates.

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