Promoting immobilization and catalytic activity of horseradish peroxidase on mesoporous silica through template micelles

New concept on the promotion of immobilization and catalytic activity of enzyme on mesoporous silica through template micelles is proposed and realized in this paper. Proper P123 templates are controllable retained in the as-synthesized SBA-15, not only to anchor the horseradish peroxidase (HRP) guest, but also to establish the crowding-like microenvironment around the enzyme. The influence of retaining templates on the pore structure of SBA-15, immobilization, and catalytic activity of HRP is studied, and the possible process of template removal is proposed. Ethanol refluxing of 6 h is conformable to prepare the optimal mesoporous support characterized with the retained templates of about 8%. With the assistance of retained templates in SBA-15, up to 49 mg g−1 of HRP can be immobilized, 100% more than that on calcined SBA-15. Furthermore, the thermal stability, the resistance of pH variation and denaturing agent urea, and the recycle usage of HRP immobilized are obviously elevated, paving a novel and low-cost route to develop enzyme catalysts.

Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (68 K)Download as PowerPoint slideHighlight► The templates of SBA-15 are exploited to make the optimal environment for enzyme. ► More HRP can be immobilized, up to 49 mg g−1, in the SBA-15 reserved P123 templates. ► Thermal stability of HRP/SBA-15 is greatly enhanced. ► The HRP immobilized kept 74% of original activity after used for 5 times. ► This new strategy converts the scrap micelles to efficient modifier for enzyme catalysis.