Publication | Closed Access
Kinetic Properties of (+)‐Catechin Oxidation by a Basic Peroxidase Isoenzyme from Strawberries
28
Citations
15
References
1997
Year
EngineeringKinetic PropertiesStrawberry PeroxidaseRedox BiologyPolyphenolicsOxidative StressPartially‐heat Stable StrawberryFood ChemistryChemical EngineeringBiochemical EngineeringRedox ChemistryPhytochemicalBiochemistryCatalysisBasic Peroxidase IsoenzymeBiomolecular EngineeringOxygen Reduction ReactionPeroxidase OxidationsPhytochemistryMedicine
ABSTRACT The ability of a partially‐heat stable strawberry ( Fragaria × ananassa ) peroxidase to oxidize (+)‐catechin was studied and its oxidation followed the accepted model for peroxidase oxidations. Compound I (CoI) and compound II (CoII) were the main intermediates in the catalytic cycle. The reactivity of strawberry peroxidase with H 2 O 2 [K 1 = 2.63 μM ‐1 s ‐1 ] and with (+)‐catechin [k 3 = 0.57 μM ‐1 s ‐1 ] suggested that (+)‐catechin is an excellent o‐diphenol for CoII reduction. The strong cooperativity of this peroxidase isoenzyme indicates its great efficacy in oxidation of (+)‐catechin at low H 2 O 2 concentrations.
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