Thermal stability of peroxidase from the african oil palm tree Elaeis guineensis

Abstract

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 À! 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.

Purification and Thermal Characterization of a Novel Peroxidase from a Local Chick Pea Cultivar

“…There are many reports of peroxidase involvement in lignin biosynthesis [2], auxin metabolism [3], disease resistance [4], wound healing and response to air pollutant stress [5] in plants. Peroxidases have also been widely used as important components of reagents for clinical diagnosis and enzyme immunoassays [6]. Some modern applications of peroxidases include the treatment of waste waters containing phenols and aromatic amines, synthesis of different aromatic chemicals and polymeric materials and removal of peroxide from materials such as food stuffs and industrial wastes [7][8][9][10].…”

“…However, peroxidases with comparable as well as higher stabilities and *Address correspondence to this author at the Industrial Biotechnology Laboratory, Department of Chemistry, University of Agriculture, Faisalabad-38040, Pakistan; Tel: +92-(041)-9200161-70/3320; Fax: +92-(041)-9200764; E-mail: hnbhatti2005@yahoo.com different substrate specificities have been isolated from Glycine max (soybean hulls) [1,16], oil palm tree [6,15], tobacco [17], strawberry [18,19] and many other fruits [20]. Therefore, the availability of highly stable and active peroxidases from sources other than horseradish roots would go a long way toward the development of a catalytic enzyme with broad commercial and environmental possibilities.…”

Thermal stability of peroxidase from Chamaerops excelsa palm tree at pH 3

“…On comparing the kinetic parameters of CEP stability at pH 3 with those of other peroxidases [17,18,21,22], it is evident that the thermostability of CEP is substantially greater than that of horseradish peroxidase isoenzyme c (HRPc) and anionic peanut (Arachis hypogaea L.) peroxidase (aPrx), and is practically the same as the stability of peroxidase from the African oil palm tree Elaeis guineensis (AOPTP) and peroxidase from royal palm tree Roystonea regia (RPTP). Thus, the T m for CEP at a scan rate of 60 K h −1 is 70.1 ± 0.2 • C while for aPrx this value is 39.4 ± 0.2 • C; for HRPc it is 60.2 ± 0.2 • C; for AOPTP it is 72.3 ± 0.2 • C and for RPTP it is 72.3 ± 0.2 • C. In row of the Arrhenius energy of activation values CEP (105.1 ± 1.7 kcal mol −1 ) close to AOPTP (103 ± 6 kcal mol −1 ) being lower RPTP (129.1 ± 0.8 kcal mol −1 ) and significantly higher in comparison those of HRPc (38.2 ± 0.5 kcal mol −1 ) and aPrx (67.9 ± 0.5 kcal mol −1 ).…”

“…Recently, peroxidases from the leaves of some tropical palm trees have been isolated and characterized [12][13][14][15]. These enzymes showed very high stability at elevated temperatures, within broad range of pH values, in the presence of hydrogen peroxide and chemical denaturants [16][17][18] that make them intriguing catalysts for industrial applications. Here we describe a detailed investigation of the thermal stability of peroxidase purified from leaves of cold-resistant palm tree Chamaerops excelsa at pH 3, by using different independent methods, such as differential scanning calorimetry (DSC), circular dichroism (CD), intrinsic fluorescence and enzymatic activity assays.…”

Steady-state kinetics of <i>Roystonea regia</i> palm tree peroxidase

“…peroxidases from other plants, such as peanut [10], barley [11], tea [12], Arabidopsis thaliana [13], and palm trees [14][15][16][17][18].…”