Zhou Xiang, Xu Jiahao, Sun Jiayao, Chen Hao, Huang Dechun, Chen Wei, Qian Hongliang
Department of Pharmaceutical Engineering, School of Engineering, China Pharmaceutical University, Nanjing, 211198, China.
Department of Pharmaceutical Engineering, School of Engineering, China Pharmaceutical University, Nanjing, 211198, China; Engineering Research Center for Smart Pharmaceutical Manufacturing Technologies, Ministry of Education, China Pharmaceutical University, Nanjing, 211198, China.
Int J Biol Macromol. 2025 Sep 7:147436. doi: 10.1016/j.ijbiomac.2025.147436.
1,3-Dioleoyl-2-palmitoylglycerol (OPO) is crucial for infant nutrition; however, conventional immobilized lipase requires high-purity enzymes, which increases costs and limits industrial scalability. Herein, Rhizomucor miehei lipase (RML) was immobilized on surface-modified magnetic nanoparticles using cross-linked enzyme aggregates (CLEAs) technology to produce FeO@SiO@TPOAC@RML CLEAs. This approach combines the separation and immobilization of enzymes, allowing for the use of lower-purity lipase, which enhances its suitability for industrial-scale processes. The optimized FeO@SiO@TPOAC@RML CLEAs exhibited excellent thermal, pH, and storage stability. The performance of FeO@SiO@TPOAC@RML CLEAs was evaluated by catalyzing the synthesis of OPO through the enzymatic hydrolysis of glycerol tripalmitate (PPP) and oleic acid (OA). Under optimal conditions, the OPO content in products reached 63.33 ± 0.30 %, highlighting the high efficiency of the enzymatic process. After eight reuse cycles, the FeO@SiO@TPOAC@RML CLEAs retained around 75 % of their relative activity. Therefore, this strategy of lipase immobilization using CLEA technology, coupled with magnetic nanoparticles, offers a promising approach for OPO synthesis.
