The heat tolerance and the inactivation kinetics of peroxidase (POD) and polyphenol oxidase (PPO) in pineapples (Ananas comosus) were studied in the temperature range $45-95^{circ}C$. The kinetic parameters, such as deactivation rate constant (k), activation energy ($E_a$), and decimal reduction rate (D) of the thermal inactivation process, were determined. POD in pineapples showed biphasic inactivation behavior at temperatures range $45-75^{circ}C$ but was monophasic at $85-95^{circ}C$. This indicate that POD has 2 isozymes, namely heat labile and heat resistant, with $E_a$ of 68.79 and 93.23 kJ/mol, respectively. On the other hand, the heat denaturation of pineapple PPO could be described as simple monophasic first-order behavior with $E_a$ of 80.15 kJ/mol. Thus, the results of this study is useful in blanching technology where it shows a shortened time with higher temperature can be applied. The determination of the heat tolerance and inactivation POD and PPO, at different temperature range as done in the present work, was very important to improve the blanching process. This also will help to optimize the pineapple canning process which is one of the most important food industries in many tropical regions.