Plant enzymes, such as those from castor bean (Ricinus communis L.), have been studied as biocatalysts for various industrial applications. In this study, a powdered enzyme extract was used to analyze the potential of lipases present in three castor bean varieties (LV1–LV3). Their hydrolytic activity was evaluated against olive and castor oil substrates (refined and non-refined) at pH 4.5 and 7.0. The results showed that LV2 had higher catalytic activity, managing to hydrolyze more than 98% of the oils in only 4.5 h of reaction. Additionally, diverse computational tools were employed to assess the behavior of OBL1 lipase. By molecular docking analysis, it was found that the binding of ricinoleic acid triacylglycerols to the catalytic site was favored at an acidic pH of 4.5 due to enhanced hydrogen bond formation. In contrast, at pH 7.0, hydrophobic interactions predominated. Molecular dynamics analyses of OBL1 showed that the enzyme–substrate complex is stable over time, providing a robust molecular explanation for the high catalytic efficiency observed in the experimental assays. This research stands out as one of the first to combine lab experiments with computational modeling to study castor bean lipases. Our integrated approach provides fresh insights into the enzyme’s versatile catalytic capabilities, underscoring its potential as a powerful and reliable tool for industrial biotechnology.