Honey Catalase: Occurrence and Some Kinetic Properties

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Abstract
There have been earlier claims of the existence of a catalase in honey, but these were based on inconclusive experiments and inappropriate methods. In the present study, a correlation of manometric and spectrophotometric findings has provided the first unequivocal evidence for the occurrence of this enzyme in honey. An investigation of some of the kinetic properties of the honey catalase revealed a pH optimum at 7–8·5 and a substrate concentration optimum at 0·018M. The Michaelis constant was 0.0154M. The effect of enzyme concentration on reaction velocity was linear. The reaction followed a first order, being dependent on the H2O2 concentration. In honey, catalase apparently serves as a control on the H2O2 equilibrium, thus regulating the activity of the honey glucose oxidase.

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