Esterases are widely used in food processing industry, but there is little information concerning enzymes involved in decompositions of esters contributing to pollution of environment. Vinyl acetate (an ester of vinyl alcohol and acetic acid) is a representative of volatile organic compounds (VOCs) in decomposition, of which hydrolyses and oxidoreductases are mainly involved. Their activities under periodically changing conditions of environment are essential for the removal of dangerous VOCs. Esterase and alcohol/aldehyde dehydrogenase activities were determined in crude cell extract from Pseudomonas fluorescens PMC 2123 after vinyl acetate induction. All examined enzymes exhibit their highest activity at 30–35 °C and pH 7.0–7.5. Esterase preferably hydrolyzed ester bonds with short fatty chains without plain differences for C2 or C4. Comparison of Km values for alcohol and aldehyde dehydrogenases for acetaldehyde suggested that this metabolite was preferentially oxidized than reduced. Activity of alcohol dehydrogenase reducing acetaldehyde to ethanol suggested that one mechanism of defense against the elevated concentration of toxic acetaldehyde could be its temporary reduction to ethanol. Esterase activity was inhibited by phenylmethanesulfonyl fluoride, while β-mercaptoethanol, dithiothreitol, and ethylenediaminetetraacetic acid had no inhibitor effect. From among metal ions, only Mg2+ and Fe2+ stimulated the cleavage of ester bond.Electronic supplementary materialThe online version of this article (doi:10.1007/s12223-013-0268-0) contains supplementary material, which is available to authorized users.
This study focuses on the phenol biodegradation kinetics by Stenotrophomonas maltophilia KB2 in a nickel-contaminated medium. Initial tests proved that a nickel concentration of 33.3 mg·L−1 caused a cessation of bacterial growth. The experiments were conducted in a batch bioreactor in several series: without nickel, at constant nickel concentration and at varying metal concentrations (1.67–13.33 g·m−3). For a constant Ni2+ concentration (1.67 or 3.33 g·m−3), a comparable bacterial growth rate was obtained regardless of the initial phenol concentration (50–300 g·m−3). The dependence µ = f (S0) at constant Ni2+ concentration was very well described by the Monod equations. The created varying nickel concentrations experimental database was used to estimate the parameters of selected mathematical models, and the analysis included different methods of determining metal inhibition constant KIM. Each model showed a very good fit with the experimental data (R2 values were higher than 0.9). The best agreement (R2 = 0.995) was achieved using a modified Andrews equation, which considers the metal influence and substrate inhibition. Therefore, kinetic equation parameters were estimated: µmax = 1.584 h−1, KS = 185.367 g·m−3, KIS = 106.137 g·m−3, KIM = 1.249 g·m−3 and n = 1.0706.
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