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Kinetic and stability study of the peroxidase inhibition in ionic liquids / Aristides P. Carneiro in Industrial & engineering chemistry research, Vol. 48 N° 24 (Décembre 2009) 

Public ISBD [article]  in Industrial & engineering chemistry research > Vol. 48 N° 24 (Décembre 2009) . - pp. 10810–10815 Titre : Kinetic and stability study of the peroxidase inhibition in ionic liquids Type de document : texte imprimé Auteurs : Aristides P. Carneiro, Auteur ; Oscar Rodriguez, Auteur ; Fatima L. Mota, Auteur Année de publication : 2010 Article en page(s) : pp. 10810–10815 Note générale : Industrial chemistry Langues : Anglais (eng) Mots-clés : Kinetic--Stability--Peroxidase--Inhibition--Ionic--Liquids Résumé : 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][MDEGSO4], 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 (Vmax) decreased with increasing concentration of IL. The effect of [emim][EtSO4] concentration on the decrease of Vmax was higher than that of [emim][MDEGSO4]. 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. ISSN : 0888-5885 En ligne : http://pubs.acs.org/doi/abs/10.1021/ie9007612 [article] Kinetic and stability study of the peroxidase inhibition in ionic liquids [texte imprimé] / Aristides P. Carneiro, Auteur ; Oscar Rodriguez, Auteur ; Fatima L. Mota, Auteur . - 2010 . - pp. 10810–10815. Industrial chemistry Langues : Anglais (eng) in Industrial & engineering chemistry research > Vol. 48 N° 24 (Décembre 2009) . - pp. 10810–10815 Mots-clés : Kinetic--Stability--Peroxidase--Inhibition--Ionic--Liquids Résumé : 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][MDEGSO4], 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 (Vmax) decreased with increasing concentration of IL. The effect of [emim][EtSO4] concentration on the decrease of Vmax was higher than that of [emim][MDEGSO4]. 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. ISSN : 0888-5885 En ligne : http://pubs.acs.org/doi/abs/10.1021/ie9007612

Kinetic and stability study of the peroxidase inhibition in ionic liquids / Aristides P. Carneiro in Industrial & engineering chemistry research, Vol. 48 N° 24 (Décembre 2009) 

Public ISBD [article]  in Industrial & engineering chemistry research > Vol. 48 N° 24 (Décembre 2009) . - pp. 10810–10815 Titre : Kinetic and stability study of the peroxidase inhibition in ionic liquids Type de document : texte imprimé Auteurs : Aristides P. Carneiro, Auteur ; Oscar Rodriguez, Auteur ; Fatima L. Mota, Auteur Année de publication : 2010 Article en page(s) : pp. 10810–10815 Note générale : Chemical engineering Langues : Anglais (eng) Mots-clés : Ionic  liquids  Peroxidase  Kinetic  study  Stability  study Résumé : 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][MDEGSO4], 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 (Vmax) decreased with increasing concentration of IL. The effect of [emim][EtSO4] concentration on the decrease of Vmax was higher than that of [emim][MDEGSO4]. 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. En ligne : http://pubs.acs.org/doi/abs/10.1021/ie9007612 [article] Kinetic and stability study of the peroxidase inhibition in ionic liquids [texte imprimé] / Aristides P. Carneiro, Auteur ; Oscar Rodriguez, Auteur ; Fatima L. Mota, Auteur . - 2010 . - pp. 10810–10815. Chemical engineering Langues : Anglais (eng) in Industrial & engineering chemistry research > Vol. 48 N° 24 (Décembre 2009) . - pp. 10810–10815 Mots-clés : Ionic  liquids  Peroxidase  Kinetic  study  Stability  study Résumé : 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][MDEGSO4], 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 (Vmax) decreased with increasing concentration of IL. The effect of [emim][EtSO4] concentration on the decrease of Vmax was higher than that of [emim][MDEGSO4]. 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. En ligne : http://pubs.acs.org/doi/abs/10.1021/ie9007612