Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin

Food Chemistry

Volumn 127, Issue 2, 2011, Pages 487-492

  Pescuma, Micaela ^a   Hébert, Elvira María ^a   Rabesona, Hanitra ^b   Drouet, Martine ^c   Choiset, Yvan ^b   Haertlé, Thomas ^b   Mozzi, Fernanda ^a   De Valdez, Graciela Font ^a,d   Chobert, Jean Marc ^b  

^a CENTRO DE REFERENCIA PARA LACTOBACILOS CERELA CONICET   (Argentina)

^b INRA   (France)

^c ANGERS UNIVERSITY HOSPITAL   (France)

^d UNIVERSIDAD NACIONAL DE TUCUMÁN   (Argentina)

Author keywords

Lactoglobulin; Allergy; Lactic acid bacteria; Lactobacillus

Indexed keywords

ALLERGIC PATIENTS; ELISA TEST; LACTIC ACID BACTERIA; LACTOBACILLUS; LACTOBACILLUS DELBRUECKII; LACTOBACILLUS STRAINS; LACTOGLOBULIN; LC-MS/MS; MILK PROTEIN; RP-HPLC; SDS-PAGE; SEQUENCE ANALYSIS; WHEY PROTEINS;

ANTIGENS; BACTERIOLOGY; BODY FLUIDS; DAIRY PRODUCTS; LACTIC ACID; PEPTIDES;

ALLERGIES;

BETA LACTOGLOBULIN; EPITOPE; IMMUNOGLOBULIN E; MILK PROTEIN;

ALLERGENICITY; ALLERGY; ANTIGEN RECOGNITION; ARTICLE; BACTERIAL STRAIN; CHILD; CLINICAL ARTICLE; CONTROLLED STUDY; HUMAN; LACTOBACILLUS DELBRUECKII; LACTOBACILLUS DELBRUECKII SUBSP BULGARICUS; PRESCHOOL CHILD; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN HYDROLYSIS; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEQUENCE ANALYSIS;

BOVINAE; LACTOBACILLUS; LACTOBACILLUS DELBRUECKII SUBSP. BULGARICUS;

EID: 79952314454     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.01.029     Document Type: Article

References (32)

1. Bernasconi, E., Fritsché, R., & Corthésy, B. (2006). Specific effects of denaturation, hydrolysis and exposure to Lactococcus lactis on bovine β-lactoglobulin trans epithelial transport, antigenicity and allergenicity. Clinical and Experimental Allergy, 36, 803-814. (Pubitemid 43972976)
2. Bertrand-Harb, C., Baday, A., Dalgalarrondo, M., Chobert, J.-M., & Haertlé, T. (2002). Thermal modifications of structure and codenaturation of α-lactalbumin and β-lactoglobulin induce changes of solubility and susceptibility to proteases. Nahrung/Food, 46, 283-289. (Pubitemid 135699452)
3. Bu, G., Luo, Y., Zhang, Y., & Chen, F. (2010). Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins. Journal of Science and Food Agriculture, 90(12), 2015-2020.
4. Davis, P. J., & Williams, S. C. (1998). Protein modification by thermal processing. Allergy, 53, 102-105. (Pubitemid 28535361)
5. Ehn, B. M., Ekstrand, B., Bengtsson, U., & Ahlstedt, S. (2004). Modification of IgE binding during heat processing of the cow's milk allergen β-lactoglobulin. Journal of Agriculture and Food Chemistry, 52, 1398-1403.
6. El-Zahar, K., Sitohy, M., Choiset, Y., Métro, F., Haertlé, T., & Chobert, J.-M. (2005). Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin. Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis. International Dairy Journal, 15, 17-27. (Pubitemid 39527113)
7. Exterkate, F. A., Alting, A. C., & Bruinenberg, P. G. (1993). Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region. Applied and Environmental Microbiology, 59, 3640-3647. (Pubitemid 23327561)
8. Hays, T., Robert, A., & Wood, M. D. (2005). A systematic review of the role of hydrolyzed infant formulas in allergy prevention. Archives of Pediatric and Adolescent Medicine, 159, 810-816. (Pubitemid 41248387)
9. Hébert, E. M., Raya, R. R., & De Giori, G. S. (2000). Nutritional requirements and nitrogen-dependent regulation of proteinase activity of Lactobacillus helveticus CRL 1062. Applied and Environmental Microbiology, 66, 5316-5321. (Pubitemid 32217136)
10. S1- and β-caseins breakdown and release of a bioactive peptide by a cell-envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581. Applied and Environmental Microbiology, 74, 3682-3689.
11. Hill, D. J., & Hosking, C. S. (1996). Cow milk allergy in infancy and early childhood. Clinical and Experimental Allergy, 26, 243-246. (Pubitemid 26100473)
12. Kim, S. B., Seo, I. S., Khan, M. A., Ki, K. S., Lee, W. S., Lee, H. J., et al. (2007). Enzymatic hydrolysis of heated whey: Iron-binding ability of peptides and antigenic protein fractions. Journal of Dairy Science, 90, 4033-4042. (Pubitemid 350045177)
13. Kleber, N., Weirich, U., & Hinrichs, J. (2006). Screening for lactic acid bacteria with potential to reduce antigenic response of β-lactoglobulin in bovine skim milk and sweet whey. Innovative Food Science and Emerging Technology, 7, 233-238. (Pubitemid 44160562)
14. Kneepkens, C. M. F., & Meijer, Y. (2009). Clinical practice. Diagnosis and treatment of cow's milk allergy. European Journal Pediatrics, 168, 891-896.
15. Mollet, B., & Rowland, I. (2002). Functional foods: At the frontier between food and pharma. Current Opinion in Biotechnology, 13, 483-485. (Pubitemid 35379935)
16. Pecquet, S., Bovetto, L., Maynard, F., & Fritsche, R. (2000). Peptides obtained by tryptic hydrolysis of bovine β-lactoglobulin induce specific oral tolerance in mice. Journal of Allergy and Clinical Immunology, 105, 514-521. (Pubitemid 30169910)
17. Pederson, J. A., Mileski, G. J., Weimer, B. C., & Steele, J. L. (1999). Genetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32. Journal of Bacteriology, 181, 4592-4597. (Pubitemid 29357941)
18. Peñas, E., Préstamo, G., Baeza, M., Martínez-Molero, M., & Gomez, R. (2006). Effect of combined high-pressure and enzymatic treatments on the hydrolysis and immunoreactivity of dairy whey proteins. International Dairy Journal, 16, 831-839.
19. Pescuma, M., Hébert, E. M., Mozzi, F., & Font de Valdez, G. (2007). Hydrolysis of whey proteins by Lactobacillus acidophilus, Streptococcus thermophilus and Lactobacillus delbrueckii subsp. bulgaricus grown in a chemically defined medium. Journal of Applied Microbiology, 103, 1738-1743.
20. Pescuma, M., Hébert, E. M., Dalgalarrondo, M., Haertlé, T., Mozzi, F., Chobert, J.-M., et al. (2009). Effect of exopolysaccharides on hydrolysis of β-lactoglobulin by Lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system. Journal of Agriculture and Food Chemistry, 57, 5571-5577.
21. Pescuma, M., Hébert, E. M., Mozzi, F., & Font de Valdez, G. (2010). Functional fermented whey-based beverage using lactic acid bacteria. International Journal of Food Microbiology, 141, 73-81.
22. Pessi, T., Isolauri, E., Sütas, Y., Kankaanranta, H., Moilanen, E., & Hurme, M. (2001). Suppression of T-cell activation by Lactobacillus rhamnosus GG-degraded bovine casein. Immunopharmacology, 1, 211-218. (Pubitemid 32183720)
23. Peyron, S., Mouécoucou, J., Frémont, S., Sanchez, C., & Gontard, N. (2006). Effects of heat treatment and pectin addition on β-lactoglobulin allergenicity. Journal of Agriculture and Food Chemistry, 54, 5643-5650. (Pubitemid 44195752)
24. Pintado, M. E., Pintado, A. E., & Malcata, F. X. (1999). Controlled whey protein hydrolysis using two alternative proteases. Journal of Food Engineering, 42, 1-13.
25. Prioult, G., Pecquet, S., & Fliss, I. (2004). Stimulation of interleukin-10 production by acidic β-lactoglobulin-derived peptides hydrolyzed with Lactobacillus paracasei NCC2461 peptidases. Clinical and Diagnostic Laboratory Immunology, 11, 266-271. (Pubitemid 38380805)
26. Prioult, G., Pecquet, S., & Fliss, I. (2005). Allergenicity of acidic peptides from bovine β-lactoglobulin is reduced by hydrolysis with Bifidobacterium lactis NCC362 enzymes. International Dairy Journal, 15, 439-448. (Pubitemid 40451655)
27. Schouten, B., van Esch, B. C. A. M., Hofman, G. A., van Doorn, S. A. C. M., Knol, J., Nauta, A. J., et al. (2009). Cow milk allergy symptoms are reduced in mice fed dietary synbiotics during oral sensitization with whey. Journal of Nutrition, 139(7), 1398-1403.
28. Selo, I., Clement, G., Bernard, H., Chatel, J. M., Cremion, C., & Peltre, G. (1999). Allergy to bovine β-lactoglobulin. Specificity of human IgE to tryptic peptides. Clinical and Experimental Allergy, 29, 1055-1063.
29. Sinha, R., Radha, C., Prakash, J., & Kaul, P. (2007). Whey protein hydrolysate: Functional properties, nutritional quality and utilization in beverage formulation. Food Chemistry, 101, 1484-1491. (Pubitemid 44466234)
30. Svenning, C., Brynhildsvold, J., Molland, T., Langsrud, T., & Vegarud, G. E. (2000). Antigenic response of whey proteins and genetic variants of β-lactoglobulin the effect of proteolysis and processing. International Dairy Journal, 10, 699-711. (Pubitemid 32169833)
31. van Beresteijn, E. C. H., Peeters, R. A., Kaper, J. G. M., Meijer, R., Robben, A. J. P. M., & Schmidt, D. G. (1994). Molecular mass distribution, immunological properties and nutritive value of whey protein hydrolysates. Journal of Food Protection, 57, 619-625.
32. Taheri-Kafrani, A., Gaudin, J.-C., Rabesona, H., Nioi, C., Agarwal, D., Drouet, M., et al. (2009). Effects of heating and glycation of β-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. Journal of Agriculture and Food Chemistry, 57, 4974-4982.