Gao_2026_Int.J.Biol.Macromol__151498

Developing a biocatalyst with both high activity and stability is crucial for the preparation of structured lipids, but this remains challenging due to the limited adaptability of traditional carriers and lipases. In this study, tannic acid (TA) coating was introduced into amino resin (AR) to create a heterofunctional platform. Then, the hydrophobicity of the carrier surface was precisely controlled by regulating the grafting amount of octadecylamine (ODA, 0.4 mmol/g AR-TA), and Rhizomucor miehei lipase (RML) was subsequently immobilized on the carrier. Compared with RML immobilized on the unmodified AR (RML@AR), the enzyme activity, thermal stability (60 degreesC for 10 h) and storage stability (4 degreesC for 60 days) of RML immobilized on the modified AR (RML@AR-TA-ODA) were significantly improved, with the values increased by 80%, 21.23% and 11.96%, respectively. Mechanically, the immobilization process of RML@AR-TA-ODA was endothermic, chemical and spontaneous, with boundary layer diffusion and intraparticle diffusion being the rate-controlling steps. RML@AR-TA-ODA achieved a medium- and long-chain triacylglycerol yield of 93.57%, with superior catalytic performance and operational stability compared to the commercial Lipozyme RM C. Consequently, this study may provide a novel strategy for the construction of immobilized lipase with high activity and stability for the green and efficient preparation of structured lipids.