| Autor: |
Qianwen Ye, Lifeng Lao, Ao Zhang, Yiman Qin, Manli Zong, Daodong Pan, Hua Yang, Zhen Wu |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Journal of Dairy Science, Vol 106, Iss 12, Pp 8207-8220 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
0022-0302 |
| DOI: |
10.3168/jds.2023-23440 |
| Popis: |
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, a novel LPxTG-motif protein with esterase activity (LEP) was expressed, and the multifunctional properties such as adhesion properties and esterase activity were also investigated. When cocultured with Limosilactobacillus reuteri SH-23, the adhesion ability of L. reuteri SH-23 to HT-29 cells was improved, and this adhesion was further found relating to the potential target protein Pyruvate kinase M1/2 (PKM) of HT-29 cells. In addition, as a multifunctional protein, LEP can promote the hydrolysis of bovine milk lipids with its esterase activity, and the activity was enhanced in the presence of Zn2+ and Mn2+ at pH 7. Furthermore, the polyunsaturated fatty acids (PUFA) 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 PUFA releasing properties of the multifunctional protein derived from L. reuteri SH-23 and shed light on the beneficial effect of this Lactobacillus strain on the colonization of the gastrointestinal tract. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
|
