Characterization of new strain Lactobacillus paracasei I-N-10 with proteolytic activity: Potential role in decrease in β-casein immuno-reactivity
| Autor: | Aynur Ahmadova, Imen Hadji Sfaxi, Thomas Haertlé, Jean-Marc Chobert, Hanitra Rabesona, Shady El-Ghaish |
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| Přispěvatelé: | Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Institut National des Sciences Appliquées et de Technologie (INSAT), Baku State University, FUNGINIB [ANR-09-ALIA-005-03], NATO [98164 SfP], French Ministry ('Service d'Action Culturelle et Scientifique' from the French Embassy in Baku), Egyptian Ministry of Foreign Affairs and Education |
| Rok vydání: | 2012 |
| Předmět: |
Proteases
food.ingredient Lactobacillus paracasei Proteolysis SUSCEPTIBILITY Biochemistry Industrial and Manufacturing Engineering Hydrolysate Epitope Microbiology Serine MILK food LACTIC-ACBACTERIA FERMENTED FOODS [SDV.IDA]Life Sciences [q-bio]/Food engineering Skimmed milk Milk allergy ANTIGENICITY medicine CELL-ENVELOPE PROTEINASE [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering LACTOCOCCUS-LACTIS WALL-BOUND PROTEINASE medicine.diagnostic_test biology POLYACRYLAMIDE-GEL ELECTROPHORESIS food and beverages General Chemistry Proteolytic activity biology.organism_classification 16S ribosomal RNA RESISTANCE Food Science Biotechnology |
| Zdroj: | European Food Research and Technology European Food Research and Technology, Springer Verlag (Germany), 2012, 235 (3), pp.447-455. ⟨10.1007/s00217-012-1772-1⟩ |
| ISSN: | 1438-2385 1438-2377 |
| DOI: | 10.1007/s00217-012-1772-1 |
| Popis: | The proteolytic activity of thirty-three Lisolates from Mongolian tarag was tested on skimmed milk. The strain displaying the highest proteolytic activity was purified and presented by 16S rDNA sequencing 99.9 % homology with Lactobacillus paracasei 1-4-2A. It was named L. paracasei I-N-10. Proteases of L. paracasei I-N-10 hydrolyze predominately beta-casein and in some level alpha(S2)-casein; hydrolysis of alpha(S1)-casein was not observed. Proteolytic activity was optimal at 42 A degrees C and neutral pH. Proteases of L. paracasei I-N-10 were inhibited by serine- and metalloproteases inhibitors. PCR amplification revealed the presence of prtP gene, which was identical to prtP gene of L. paracasei genus. Mass spectrometry analysis of beta-casein hydrolysate allowed to characterize 7 peptides resulting from proteolysis by L. paracasei I-N-10. The isolated strain was able to cleave beta-casein in different sites including 2 of the major linear epitopes implicated in its allergenicity. Being sensitive to main antibiotics classes, L. paracasei I-N-10 could be considered as safe and used as starter culture with a potential role in decreasing beta-casein immuno-reactivity. |
| Databáze: | OpenAIRE |
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