Peroxidase biocatalysis in water-soluble ionic liquids: activity, kinetic and thermal stability
authors Tavares, APM; Rodriguez, O; Macedo, EA
nationality International
journal BIOCATALYSIS AND BIOTRANSFORMATION
author keywords enzyme activity; ionic liquids; peroxidase; thermal stability; kinetic
keywords HORSERADISH-PEROXIDASE; POLYPHENOL OXIDASE; ENZYME-ACTIVITY; INACTIVATION; STABILIZATION; INHIBITION; PARAMETERS; CATALYSIS; REMOVAL; LACCASE
abstract The activity and stability of commercial peroxidase was investigated in the presence of five 1-alkyl-3-methylimidazolium-based ionic liquids (ILs) with either bromide or chloride anions: [C(x)mim][X]. The peroxidase activity and stability were better for the shorter alkyl chain lengths of the ILs and peroxidase was more stable in the presence of the bromide anion, rather than chloride. The thermal inactivation profile was studied from 45 to 60 degrees C in [C(4)mim][Cl] and [C(4)mim][Br]. The activation energy was also determined. Kinetic analysis of the enzyme in the presence of the [C(4)mim][Br] or control (buffer solution) showed that the K-M value increased 5-fold and Vm decreased 13-fold in the presence of the IL. The increase in K-M indicates that this IL can reduce the binding affinity between substrate and enzyme.
publisher INFORMA HEALTHCARE
issn 1024-2422
year published 2012
volume 30
issue 4
beginning page 417
ending page 425
digital object identifier (doi) 10.3109/10242422.2012.715636
web of science category Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology
subject category Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology
unique article identifier WOS:000309287300006
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journal impact factor 1.863
5 year journal impact factor 1.598
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