TAILIEUCHUNG - Báo cáo Y học: Thermal stability of peroxidase from the african oil palm tree Elaeis guineensis

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 | Eur. J. Biochem. 269 2584-2590 2002 FEBS 2002 doi Thermal stability of peroxidase from the african oil palm tree Elaeis guineensis Anabel Rodríguez1 David G. Pina1 Belén Yelamos2 John J Castillo León3 Galina G. Zhadan1 B B B Enrique Villar1 Francisco Gavilanes2 Manuel Gb Roig4 Ivan Yu. Sakharov5 and Valery Lb Shnyrov1 1Departamento de Bioquimica y Biologia Molecular Facultad de Biologia Universidad de Salamanca Salamanca Spain 2Departamento de Bioquimica y Biologia Molecular Facultad de Quimica Universidad Complutense Madrid Spain 3Escuela de Quimica Universidad Industrial de Santander Bucaramanga Colombia 4Departamento de Quimica Fisica Facultad de Quimica Universidad de Salamanca Salamanca Spain 5Department of Chemical Enzymology Faculty of Chemistry Moscow State University Moscow Russia The thermal stability of peroxidase from leaves of the African oil palm tree Elaeis guineensis AOPTP at pH was studied by differential scanning calorimetry DSC intrinsic fluorescence CD and enzymatic assays. The sperlral parameters as monitored by ellipticity changes in the far-UV CD spectrum of the enzyme as well as the increase in tryptophan intensity emission upon heating together with changes in enzymatic activity with temperature were seen to be good complements to the highly sensitive but integral method of data obtained in this i n vestiga ti o n show that thermal denaturation of palm peroxidase is an irreversible process under kinetic control that can be satisfactorily described by the two-state kinetic scheme N D where k is a first-order kinetic constant that changes with temperature as given by the Arrhenius equation N is the native state and D is the denatured state. On the basís of this model the parameters of the Arrhenius equation were calculated. Keywords peroxidase differential scanning calorimetry intrinsic fluorescence circular dichroism protein stability. Peroxidases EC donor hydrogen-peroxide .

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