Kinetic and Stability Study of the Peroxidase Inhibition in Ionic Liquids
authors Carneiro, AP; Rodriguez, O; Mota, FL; Tavares, APM; Macedo, EA
nationality International
journal INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH
keywords HORSERADISH-PEROXIDASE; ORGANIC-SOLVENTS; PHYSICAL-PROPERTIES; FUNGAL PEROXIDASES; WATER; BIOCATALYSIS; SUBSTRATE; MIXTURES; CATALYSIS; ENZYMES
abstract The activity and stability of peroxidase in aqueous solutions of two ionic liquids (ILs) have been studied. The ILs selected were 1-ethyl-3-methylimidazolium 2-(2-methoxyethoxy) ethylsulfate, [emim][MDEGSO(4)], and 1-ethyl-3-methylimidazolium ethylsulfate, [emim][EtSO4]. Experiments were performed at room temperature using concentrations of ILs between 5 and 50% (v/v) and pH values in the range from 5 to 9. The initial activity of the enzyme in these ILs at optimized conditions (pH 7 and 5-10% IL) was similar or higher than that achieved with buffer solution. Kinetic studies showed that maximum reaction Velocity (V-max) decreased with increasing concentration of IL. The effect of [emim][EtSO4] concentration on the decrease of V-max was higher than that of [emim][MDEGSO(4)]. It was found that [emim][EtSO4] was a more potent inhibitor on peroxidase activity. The peroxidase studied was active in the ILs investigated, and the enzyme exhibited a higher stability in ILs at the optimized conditions. Kinetic studies showed that inhibition was a noncompetitive type in both ILs.
publisher AMER CHEMICAL SOC
issn 0888-5885
year published 2009
volume 48
issue 24
beginning page 10810
ending page 10815
digital object identifier (doi) 10.1021/ie9007612
web of science category Engineering, Chemical
subject category Engineering
unique article identifier WOS:000272396300009
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journal analysis (jcr 2019):
journal impact factor 3.573
5 year journal impact factor 3.684
category normalized journal impact factor percentile 69.58
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