ИСТИНА

Use of hydrophilic ILs (1-butyl-2-methylimidazolium ([BMIm]) and N-butyl-3-methylpyridinium ([BMPy]) tetrafluoroborates instead of polar organic solvents (acetonitril, DMSO, and etc.) and the optimization of the reaction medium composition provided the oxidation of phenolic compounds catalyzed by plant peroxidases isolated from horseradish roots (HRP) and soybean hulls (SBP) in the presence of 60 – 80 vol% of IL. As a result, the procedures for the determination of 3x10-6 M – 3 mM of the indicated substrates in samples with low water content (pharmaceuticals, for example) were developed. The catalytic activity of the considered plant peroxidases controlled by spectrophotometric method, and their substrate specificity were ofund to depend significantly on the nature of the enzyme, IL cation, and buffer solution used as co-solvent for IL. Thus, SBP had the greatest catalytic activity and substrate specificity towards guaiacol, whereas HRP was more preferable for the transformation of o-chlorophenol in [BMIm][BF4]-water mixture (70:30 vol%). The conditions of the formation, storage and applicability of the novel composite {cellulose-[BMIm][Cl]-peroxidase} in the reactions of aryldiamines (o-phenylendiamine, o-dianisidine, 3,3’,5,5’-tetramethylbensidine, TMB) and catecholamines (dopamine, adrenaline, alfa-methyldopa, dobutamine) oxidation by H2O2 were optimized.