Peroxidases are ubiquitous enzymes that catalyze a variety of oxygen-transfer reactions and are thus potentially useful for industrial and biomedical applications. Over the last decade, several studies have shown that peroxidases isolated from the leaves of different kinds of palm  trees such as the royal palm (Roystonea regia), the date palm (Phoenix dactylifera), the African oil palm (Elaeis guineensis), the ruffle palm (Aiphanes cariotifolia) and the windmill palms (Trachycarpus fortunei and Chamaerops excelsa) exhibit higher activity and stability than commercially available peroxidases isolated from, for example, horseradish roots (Armoracia rusticana) and soybean (Glycine max). Here, the structure, thermal denaturation, and the catalytic cycle of peroxidases from palm trees are reviewed and compared with those of other plant peroxidases. In addition, we report the biotechnological potential of palm peroxidases and their implications in cellular aging and diseases, such as Refsum’s and Alzheimer’s diseases. This paper summarizes the main characteristics of the palm peroxidases studied.