Immobilization of bacterial feruloyl esterase on mesoporous silica particles and enhancement of synthetic activity by hydrophobic-modified surface.

•Screening synthetic ability of bacterial feruloyl esterases immobilized on SBA-15.•The immobilized BFae2 from Butyrivibrio sp. showed the highest synthetic activity.•Pore size close to BFae2 dimension was optimum for synthetic activity of BFae2.•Immobilization of BFae2 on octyl-modified surface produced 70% mol BFA.•Modulation of pore size and hydrophobic surface are essential for optimum activity.