Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases
Immunoreactive gluten peptides that are not digested by peptidases produced by humans can trigger celiac disease, allergy and non-celiac gluten hypersensitivity. The aim of this study was to evaluate the ability of selected probiotic strains to hydrolyze immunoreactive gliadin peptides and to identi...
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| Format: | Article |
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MDPI AG
2024-03-01
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| Series: | Nutrients |
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| Online Access: | https://www.mdpi.com/2072-6643/16/7/976 |
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| author | Joanna Leszczyńska Agnieszka K. Szczepankowska Iwona Majak Dorota Mańkowska Beata Smolińska Sylwia Ścieszka Anna Diowksz Bożena Cukrowska Tamara Aleksandrzak-Piekarczyk |
| author_facet | Joanna Leszczyńska Agnieszka K. Szczepankowska Iwona Majak Dorota Mańkowska Beata Smolińska Sylwia Ścieszka Anna Diowksz Bożena Cukrowska Tamara Aleksandrzak-Piekarczyk |
| author_sort | Joanna Leszczyńska |
| collection | DOAJ |
| description | Immunoreactive gluten peptides that are not digested by peptidases produced by humans can trigger celiac disease, allergy and non-celiac gluten hypersensitivity. The aim of this study was to evaluate the ability of selected probiotic strains to hydrolyze immunoreactive gliadin peptides and to identify peptidase-encoding genes in the genomes of the most efficient strains. Residual gliadin immunoreactivity was measured after one- or two-step hydrolysis using commercial enzymes and bacterial peptidase preparations by G12 and R5 immunoenzymatic assays. Peptidase preparations from <i>Lacticaseibacillus casei</i> LC130, <i>Lacticaseibacillus paracasei</i> LPC100 and <i>Streptococcus thermophilus</i> ST250 strains significantly reduced the immunoreactivity of gliadin peptides, including 33-mer, and this effect was markedly higher when a mixture of these strains was used. In silico genome analyses of <i>L. casei</i> LC130 and <i>L. paracasei</i> LPC100 revealed the presence of genes encoding peptidases with the potential to hydrolyze bonds in proline-rich peptides. This suggests that <i>L. casei</i> LC130, <i>L. paracasei</i> LPC100 and <i>S. thermophilus</i> ST250, especially when used as a mixture, have the ability to hydrolyze immunoreactive gliadin peptides and could be administered to patients on a restricted gluten-free diet to help treat gluten-related diseases. |
| first_indexed | 2024-04-24T10:37:35Z |
| format | Article |
| id | doaj.art-14919ed799614b9ba44232c138ecd36f |
| institution | Directory Open Access Journal |
| issn | 2072-6643 |
| language | English |
| last_indexed | 2024-04-24T10:37:35Z |
| publishDate | 2024-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Nutrients |
| spelling | doaj.art-14919ed799614b9ba44232c138ecd36f2024-04-12T13:24:16ZengMDPI AGNutrients2072-66432024-03-0116797610.3390/nu16070976Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related DiseasesJoanna Leszczyńska0Agnieszka K. Szczepankowska1Iwona Majak2Dorota Mańkowska3Beata Smolińska4Sylwia Ścieszka5Anna Diowksz6Bożena Cukrowska7Tamara Aleksandrzak-Piekarczyk8Institute of Natural Products and Cosmetics, Faculty of Biotechnology and Food Sciences, Łódź University of Technology, Stefanowskiego 2/22, 90-530 Łódź, PolandInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, PolandInstitute of Technology and Food Analysis, Faculty of Biotechnology and Food Sciences, Łódź University of Technology, Stefanowskiego 2/22, 90-530 Łódź, PolandInstitute of Natural Products and Cosmetics, Faculty of Biotechnology and Food Sciences, Łódź University of Technology, Stefanowskiego 2/22, 90-530 Łódź, PolandInstitute of Natural Products and Cosmetics, Faculty of Biotechnology and Food Sciences, Łódź University of Technology, Stefanowskiego 2/22, 90-530 Łódź, PolandInstitute of Fermentation Technology and Microbiology, Faculty of Biotechnology and Food Sciences, Łódź University of Technology, Wólczańska 171/173, 90-530 Łódź, PolandInstitute of Fermentation Technology and Microbiology, Faculty of Biotechnology and Food Sciences, Łódź University of Technology, Wólczańska 171/173, 90-530 Łódź, PolandImmunology Laboratory, Department of Pathomorphology, The Children’s Memorial Health Institute, Dzieci Polskich 20, 04-760 Warsaw, PolandInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, PolandImmunoreactive gluten peptides that are not digested by peptidases produced by humans can trigger celiac disease, allergy and non-celiac gluten hypersensitivity. The aim of this study was to evaluate the ability of selected probiotic strains to hydrolyze immunoreactive gliadin peptides and to identify peptidase-encoding genes in the genomes of the most efficient strains. Residual gliadin immunoreactivity was measured after one- or two-step hydrolysis using commercial enzymes and bacterial peptidase preparations by G12 and R5 immunoenzymatic assays. Peptidase preparations from <i>Lacticaseibacillus casei</i> LC130, <i>Lacticaseibacillus paracasei</i> LPC100 and <i>Streptococcus thermophilus</i> ST250 strains significantly reduced the immunoreactivity of gliadin peptides, including 33-mer, and this effect was markedly higher when a mixture of these strains was used. In silico genome analyses of <i>L. casei</i> LC130 and <i>L. paracasei</i> LPC100 revealed the presence of genes encoding peptidases with the potential to hydrolyze bonds in proline-rich peptides. This suggests that <i>L. casei</i> LC130, <i>L. paracasei</i> LPC100 and <i>S. thermophilus</i> ST250, especially when used as a mixture, have the ability to hydrolyze immunoreactive gliadin peptides and could be administered to patients on a restricted gluten-free diet to help treat gluten-related diseases.https://www.mdpi.com/2072-6643/16/7/976celiac diseasegluten-related diseasesgluten-free dietendopeptidase33-mer peptidepeptidase-encoding genes |
| spellingShingle | Joanna Leszczyńska Agnieszka K. Szczepankowska Iwona Majak Dorota Mańkowska Beata Smolińska Sylwia Ścieszka Anna Diowksz Bożena Cukrowska Tamara Aleksandrzak-Piekarczyk Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases Nutrients celiac disease gluten-related diseases gluten-free diet endopeptidase 33-mer peptide peptidase-encoding genes |
| title | Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases |
| title_full | Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases |
| title_fullStr | Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases |
| title_full_unstemmed | Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases |
| title_short | Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases |
| title_sort | reducing immunoreactivity of gluten peptides by probiotic lactic acid bacteria for dietary management of gluten related diseases |
| topic | celiac disease gluten-related diseases gluten-free diet endopeptidase 33-mer peptide peptidase-encoding genes |
| url | https://www.mdpi.com/2072-6643/16/7/976 |
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