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Activation and immobilization of lipase in the multicomponent interfacial system

Journal 2026 · IF 10.6 · 发表于 2026 年 10 月 13 日
作者: Jinchao Hou,Haohua Hu,Shuaiqi Yan,Le Zhong,Geling Kuang,Yuxiao Feng,Hongwu Wang,Jiandong Cui
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摘要

A green DES/TX-100/water multicomponent interfacial system was constructed for lipase immobilization. • Hydrophobic hollow bowl-shaped mesoporous carbon (H-HBMC) served as an interfacial activation support. • AOL@H-HBMC-L/DTW achieved 108.43% activity recovery and 1.75-fold higher k cat / K m. • The interface induced lid opening, hydrophobic surface exposure, catalytic triad rearrangement, and enhanced organic solvent/thermal stability. Lipase has a wide range of applications in the food industry, such as baked food, dairy products, and oil modification. However, natural free lipase exhibits the poor stability and low activityin in dustrial applications. Inspired by the interfacial catalysis of lipase, herein, lauric anhydride-modified hydrophobic SiO 2 -derived hollow bowl-shaped mesoporous carbon particles (HBMC) were prepared and utilized to immobilize lipase from Aspergillus oryzae (AOL) in a multicomponent interfacial system composed of Deep eutectic solvents/Triton X-100/water (DTW). The resultant immobilized lipase (AOL@H-HBMC-L/DTW) exhibited higher activity recovery (108.43%) than free lipase. Meanwhile, the catalytic efficiency ( k cat / K m ) of immobilized lipase was 1.75-fold that of free lipase. In addition, thermal stability and organic solvent tolerance were also enhanced. After heating at 55 °C for 25 min, the immobilized lipase could retain 41.87% of its initial activity, whereas free lipase only maintained 29.63% of its initial activity. After dimethylformamide (DMF) treatment for 1 h, the free lipase retained only 50.12% of its activity, whereas the immobilized lipase retained 90.14%. Furthermore, it was demonstrated that hydrophobic H-HBMC-L and the multicomponent interfacial system could facilitate lipase activation and improve its activity. Therefore, we believe that the strategy proposed here has potential in preparing lipase biocatalysts with high activity and stability. Download: Download high-res image (203KB) Download: Download full-size image