“…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 ).…”