Multifunctional properties of the transmembrane LPxTG-motif protein derived from Limosilactobacillus reuteri SH-23

Abstract

Abstract The LPxTG-motif protein is an important transmembrane protein with high hydrophilicity and stability, as evidenced by its stress tolerance and adhesion ability. In this study, the multifunctional properties of a novel LPxTG-motif protein with esterase activity (LEP) were revalued. When co-cultured with Limosilactobacillus reuteri (L. reuteri) SH-23, it improved the adhesion ability of L. reuteri SH-23 to HT-29 cells, and the HT-29 cells’ adhesion related target proteins were ANXA2, CSNK1D, PKM, and HSPA8. In addition, as a multifunctional protein, LEP demonstrated potential esterase activity in the presence of Zn2+ and Mn2+ at pH 7. Furthermore, LEP, with its esterase activity, promoted the hydrolysis of bovine milk lipids. Polyunsaturated fatty acids (PUFAs) such as linoleic acid and eicosapentaenoic acid were found to increase during the hydrolyzing process. These unique properties of LEP provide a comprehensive understanding of the adhesion function and PUFAs releasing properties of the multifunctional protein derived from L. reuteri SH-23 and shed light on the beneficial effect of this Lactobacillus strain during the colonization of the gastrointestinal tract.