Thermal stability of peroxidase from the african oil palm tree Elaeis guineensis.
The thermal stability of peroxidase from leaves of the African oil palm tree Elaeis guineensis (AOPTP) at pH 3.0 was studied by differential scanning calorimetry (DSC), intrinsic fluorescence, CD and enzymatic assays. The spectral 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 DSC. The data obtained in this investigation 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 -->(k) 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 basis of this model, the parameters of the Arrhenius equation were calculated.
Rodríguez
Anabel
A
Departamento de Bioquímica y Biología Molecular, Facultad de Biología, Universidad de Salamanca, Salamanca, Spain.
Pina
David G
DG
Yélamos
Belén
B
Castillo León
John J
JJ
Zhadan
Galina G
GG
Villar
Enrique
E
Gavilanes
Francisco
F
Roig
Manuel G
MG
Sakharov
Ivan Yu
IY
Shnyrov
Valery L
VL
D028023:Arecaceae / Q000201:enzymology*; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004795:Enzyme Stability; D006358:Hot Temperature; D009195:Peroxidase / Q000737:chemistry*; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence
D009195:Peroxidase