The thermal stabilityofperoxidase fromleavesof theAfrican oil palm treeElaeis guineensis(AOPTP) at pH was studied by differential scanning calorimetry (DSC), intrinsic fluorescence, CD and enzymatic spectral parameters asmonitoredby ellipticity changes in the far-UV CD spectrum of the enzyme as well as the increase in tryp-tophan intensity emission upon heating, together with changes in enzymatic activity with temperature were seen to be good complements to the highly sensitive but integral methodofDSC
