Enhancing the Catalytic Performance of <italic>Candida antarctica</italic> Lipase B by Immobilization onto the Ionic Liquids Modified SBA‐15.

In this study, mesoporous silica SBA‐15 is modified by imidazole based ionic liquids (IL) with three different side‐chain length of cations and two different anions. Prepared supports (IL‐SBA‐15) are characterized by small‐angle powder X‐ray diffraction (XRD), X‐ray photoelectron spectroscopy (XPS) as well as Fourier transform infrared (FT‐IR), and then used to immobilize <italic>Candida antarctica</italic> lipase B (CALB). The enzymatic properties of the obtained IL‐SBA‐15‐CALB are evaluated, and the catalytic selectivity toward diacylglycerols (DAG) production in glycerolysis of triacylglycerols (TAG) reaction is also studied. Compared with the parent SBA‐15 immobilized CALB (SBA‐15‐CALB), the IL modification gives a maximum improvement of enzymatic activity from 1855 to 5044 U g⁻¹; in addition, the selectivity toward the diacylglycerols (DAG) production also increases, with the DAG/MAG ratio increasing from 3.72 to 11.99, and the DAG content increasing from 53.6 to 67.2 wt%. <italic>Practical applications</italic>: Immobilization of lipases facilitates the separation of products and the recovery of lipases for reuse. The present study shows that CALB immobilized on the IL modified SBA‐15 is potential for DAG production through glycerolysis, due to its considerable reusability as well as its high glycerolysis activity and selectivity toward DAG production, it could be considered for practical applications. Glycerolysis of corn oil catalyzed by ionic liquids modified SBA‐15 supports CALB to produce diacylglycerols. SBA‐15 is modified by ionic liquids, and then employed as carrier for <italic>Candida antarctica</italic> lipase B (CALB) immobilization. The obtained solid lipases are used to catalyze glycerolysis for diacylglycerols (DAG) production. Compared with the parent SBA‐15 immobilized CALB (SBA‐15‐CALB), ionic liquids modification gives a maximum improvement of enzymatic activity from 1855 to 5044 U g⁻¹; in addition, the selectivity toward the DAG production is also increased, with the DAG/MAG ratio increasing from 3.72 to 11.99, and the DAG content increasing from 53.6 to 67.2 wt%. [ABSTRACT FROM AUTHOR]