Specifically, a set of mesoporous silicas was modified with glyoxyl groups to immobilize covalently the FDH obtained from Candida boidinii. Three types of mesoporous silicas with different textural properties were synthesized and used as supports: i) SBA-15 (D-P = 4 nm); ii) MCF with 0.5 wt% mesitylene/pluronic ratio (D-P = 20 nm) and iii) MCF with 0.75 wt% mesitylene/pluronic ratio (D-P = 25 nm). As a whole, the immobilized FDH on MCF0.75 exhibited higher thermal stability than the free enzyme, with 75% of residual activity after 24 h at 50 degrees C. FDH/MCF0.5 exhibited the best immobilization yields: 69.4% of the enzyme supplied was covalently bound to the support. Interestingly, the specific activity increased as a function of the pore size of support and then the FDH/MCF0.75 exhibited the highest specific activity (namely, 1.05 IU/g(MCF0.75)) with an immobilization yield of 52.1%. Furthermore, it was noted that the immobilization yield and the specific activity of the FDH/MCF0.75 varied as a function of the supported enzyme: as the enzyme loading increased the immobilization yield decreased while the specific activity increased. Finally, the reuse test has been carried out, and a residual activity greater than 70% was found after 5 cycles of reaction. (c) 2021 Published by Elsevier B.V.