The core neutralizing epitope (COE) region of porcine epidemic diarrhea virus (PEDV) plays an important role in the development of the subunit vaccine against PEDV infection. To enhance the vaccine's immunogenicity, Escherichia coli heat-labile enterotoxin B (LTB) has usually been adopted as a molecular adjuvant. In this study, the COE and LTB-COE genes were engineered into the Lactobacillus -Escherichia coli shuttle vectors pSAPG1 (surface-displaying) and pSAPG2 (secreting) followed by electrotransformation into Lactobacillus casei (Lc) to yield the following recombinant strains: Lc:PG1-LTB-COE, Lc:PG2-LTB-COE, Lc:PG1-COE, and Lc:PG2-COE. Our results showed that mice immunized orogastrically with L. casei expressing COE or LTB-COE produced secretory immunoglobulin A and immunoglobulin G with the ability to neutralize PEDV in sera and mucus. Moreover, higher levels of interleukin-4 and gamma interferon were also exhibited compared with negative control. These data displayed the tendency of Lc:PG2-LTB-COE > Lc:PG1-LTB-COE > Lc:PG2-COE > Lc:PG1-COE at the same time point. Taken together, LTB-COE is more suitable for Lactobacillus expressing system to engineer mucosal vaccine against PEDV infection.