Multifunctional enzymes have the potential to enhance hydrolytic efficiency and reduce enzyme cost. In this study, by optimizing linker peptide identity and the order of fusion partners, an efficient trifunctional xylanase/glucanase/feruloyl esterase, named Xyn(Glu)A/FaeB-L1, was obtained through associating the Bacillus bifunctional xylanase/glucanase Xyn(Glu)A with its cognate feruloyl esterase FaeB using a flexible linker peptide (L1). In comparison to the parental enzymes, Xyn(Glu)A/FaeB-L1 displayed similar pH optima for enzyme activity, shifting no more than a single unit. However, the optimal reaction temperature was 5-10 °C lower than that of the parental enzymes. Intriguingly, its catalytic efficiencies (k