1. Increase of the adhesion ability and display of a rumen fungal xylanase on the cell surface of Lactobacillus casei by using a listerial cell-wall-anchoring protein.
- Author
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Hsueh HY, Yu B, Liu CT, and Liu JR
- Subjects
- Animals, Avena metabolism, Bacterial Proteins genetics, Caco-2 Cells, Cell Wall metabolism, Food Additives, Fungal Proteins metabolism, Humans, Lacticaseibacillus casei genetics, Listeria monocytogenes genetics, Probiotics, Recombinant Proteins metabolism, Rumen, Transformation, Genetic, Xylans metabolism, Xylosidases genetics, Bacterial Adhesion, Bacterial Proteins metabolism, Genes, Bacterial, Intestinal Mucosa metabolism, Lacticaseibacillus casei enzymology, Listeria monocytogenes enzymology, Xylosidases metabolism
- Abstract
Background: Lactobacillus, which has great adhesion ability to intestinal mucosa and is able to hydrolyse plant cell walls, can be used more efficiently as a feed additive. To increase the adhesion ability and display a fungal xylanase on the cell surface of Lactobacillus casei, the Listeria monocytogenes cell-wall-anchoring protein gene, mub, was introduced into L. casei ATCC 393 cells and used as a fusion partner to display the rumen fungal xylanase XynCDBFV on the cell surface of the transformed strains., Results: The transformed strain L. casei pNZ-mub, which harboured mub gene, displayed recombinant Mub on its cell surface and showed greater adhesion ability to Caco-2 cells than the parental strain. The transformed strain L. casei pNZ-mub/xyn, which harboured mub-xynCDBFV fusion gene, acquired the capacity to break down oat spelt xylan and exhibited greater competition ability against the adhesion of L. monocytogenes to Caco-2 cells, in comparison with the parental strain., Conclusion: Mub has a potential to be used as a fusion partner to display heterologous proteins on the cell surface of Lactobacillus. Moreover, this is the first report of the successful display of xylanase on the cell surface of Lactobacillus., (© 2013 Society of Chemical Industry.)
- Published
- 2014
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