Aquaporins (AQPs) are intrinsic membrane proteins responsible for facilitating water transport across biological membranes. AQPs found in plant membrane vesicles (MV) have been related to the functionality and stability of the vesicles. In this study, we focused on AQPs obtained from Brassica oleracea var. L. italica (broccoli) by the great potential for different biotechnological applications. To gain further insight into the role of AQPs in MV and advance the biotechnological applications of AQPs, we describe the heterologous overexpression of two broccoli AQPs (BoPIP1;2 and BoPIP2;2) in Pichia pastoris, resulting in the purification of both AQPs with high yield (0.14 and 0.99 mg per gram cells for BoPIP1;2 and BoPIP2;2, respectively). We reconstituted purified AQPs in liposomes to study their functionality, showing no changes in size compared to liposomes. BoPIP2;2 facilitated water transport, which was preserved for seven days at 4oC and 25ºC but not at 37oC, whereas BoPIP1;2 did not enhance water transport across the proteoliposome membrane. Additionally, BoPIP2;2 was incorporated into liposomes to encapsulate a resveratrol extract in proteoliposome vesicles, resulting in increased entrapment efficiency compared to conventional liposomes. Molecular docking identified potential binding sites for resveratrol in PIP2s, highlighting the role of AQPs in the improved entrapment efficiency of resveratrol. Moreover, a modelling study was conducted, demonstrating interactions between a plant AQP and human integrin, which may be a benefit to increase contact and internalization by the human target cells. Thus, our results suggest that AQPs-based alternative encapsulation systems can be used in specifically target biotechnological applications.