Inhibition of membrane bound lipophilic plant (Borassus flabelifer L.) peroxidase by phenolic compounds.

Borassus flabelifer peroxidase was ionically interacting with stone parts of its fruit. The apparently homogeneous membrane bound peroxidase was reversibly inhibited by various aromatic alcohols. Dixon plot clearly showed mixed type of inhibition. Ki values of peroxidase-inhibitor complexes were determined. The homogenous peroxidase had non-covalently interacting triglycerides or triglyceride esterified phytosterols. This Peroxidase was interacting with acid hydrolysable low density lipoprotein but not with high density lipoprotein. This may be one of the reasons for its stability and catalysis in organic solvents. Further studies may prove it as lipophilic enzyme. These waste stone parts may be utilized in extracting phytosterols and fatty acids which has medicinal value.