Enzymatic esterification of phytosterols is essential for their stability and bioavailability in lipophilic foods. In this study, we created a new polydopamine-based bowl-like mesoporous carrier (BLM-PDA) for lipase loading and catalyzed the esterification of phytosterols and oleic acid to produce oleate sterol ester. Candida rugosa lipase (CRL) was selected to immobilize the polymer using physical adsorption. SEM, TEM, XRD, TGA, XPS, FT-IR, and BET were used to characterize it in order to confirm the successful preparation. These less-studied asymmetric bowl-like particles showed much enhanced performance in all aspects. According to the findings, BLM-PDA had a lipase loading of around 126.05 mg g −1 , and the thermal stability and reusability of BLM-PDA@CRL fared particularly well in activity tests. After 55 h, the catalyst successfully completed the oleate sterol ester yield of 81.07% of the transesterification cycle at 40 °C. Therefore, it offers more suggestions for using an immobilized lipase nanoreactor to the biosynthesis of sterol esters.