Detoxification of sulfur mustard by enzyme-catalyzed oxidation using chloroperoxidase

• Chloroperoxidase (CPO) accelerates disposal of sulfur mustard from water solutions.
• We optimized the conditions of enzymatic oxidation of sulfur mustard (SM).
• We found that the enzymatic oxidation of SM is of a pseudo-first order.
• Determined Michaelis constant for the system: CPO–SM–H2O2 is 1.87 × 10−3 mol dm−3.

One of the most interesting methods for the detoxification of sulfur mustard is enzyme-catalyzed oxidation. This study examined the oxidative destruction of a sulfur mustard by the enzyme chloroperoxidase (EC 1.11.1.10). Chloroperoxidase (CPO) belongs to a group of enzymes that catalyze the oxidation of various organic compounds by peroxide in the presence of a halide ion. The enzymatic oxidation reaction is affected by several factors: pH, presence or absence of chloride ion, temperature, the concentrations of hydrogen peroxide and enzyme and aqueous solubility of the substrate. The optimum reaction conditions were determined by analyzing the effects of all factors, and the following conditions were selected: solvent, Britton–Robinson buffer (pH = 3) with tert-butanol (70:30 v/v); CPO concentration, 16 U/mL; hydrogen peroxide concentration, 40 mmol/L; sodium chloride concentration, 20 mmol/L. Under these reaction conditions, the rate constant for the reaction is 0.006 s−1. The Michaelis constant, a measure of the affinity of an enzyme for a particular substrate, is 1.87 × 10−3 M for this system. The Michaelis constant for enzymes with a high affinity for their substrate is in the range of 10−5 to 10−4 M, so this value indicates that CPO does not have a very high affinity for sulfur mustard.

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