ABSTRACT
In Sub-Saharan Africa, Lagenaria siceraria is an oleaginous cucurbit widely consumed for its edibleseeds. These seeds were previously categorized as good enzyme sources, including four non-specific acidphosphatases isolated and designated as BLsAP1, BLsAP2, RLsAP1, and RLsAP2. In this study, we investigateon the kinetic and thermodynamic characteristics of these biocatalysts in order to evaluate their thermostability.Thermal inactivation was carried out in the temperature range of 55°C to 80°C from 5 to 60 minutes. The resultsrevealed that thermal inactivation of studied acid phosphatases follows first order kinetics. At their optimumtemperatures, these enzymes showed high half-lives ranging from 169.06 to 495.10 minutes and D valuesfrom 561.71 to 1,645.03 minutes. Moreover, they exhibited high activation energies (from 155.08 to 200.55kJ/mol) and average enthalpy values (from 152.23 to 197.74 kJ.mol−1) suggesting their good thermostability.The comparison of all these values revealed that the two acid phosphatases (RLsAP1 and RLsAP2) from theround-fruited cultivar of L. siceraria showed better thermal stability than those (BLsAP1 and BLsAP2) fromthe blocky-fruited cultivar.