메뉴 건너뛰기




Volumn 50, Issue 2, 2015, Pages 356-364

Peptic hydrolysis of bovine beta-lactoglobulin under microwave treatment reduces its allergenicity in an ex vivo murine allergy model

Author keywords

Allergy; Balb c; Bovine beta lactoglobulin; Microwaves; Milk proteins; Pepsin hydrolysis

Indexed keywords

ALLERGENS; ALLERGIES; BIOLOGICAL MATERIALS; CHLORINE COMPOUNDS; DICHROISM; HYDROLYSIS; IRRADIATION; MAMMALS; MICROWAVE HEATING; MICROWAVES; PROTEINS;

EID: 85027951966     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/ijfs.12653     Document Type: Article
Times cited : (33)

References (35)
  • 1
    • 17644408352 scopus 로고    scopus 로고
    • Peanut- and cow's milk-specific IgE, Th2 cells and local anaphylactic reaction are induced in Balb/c mice orally sensitized with cholera toxin
    • Adel-Patient, K., Bernard, H., Ah-Leung, S., Créminon, C. & Wal, J.M. (2005). Peanut- and cow's milk-specific IgE, Th2 cells and local anaphylactic reaction are induced in Balb/c mice orally sensitized with cholera toxin. Allergy, 60, 658-664.
    • (2005) Allergy , vol.60 , pp. 658-664
    • Adel-Patient, K.1    Bernard, H.2    Ah-Leung, S.3    Créminon, C.4    Wal, J.M.5
  • 6
    • 17144373268 scopus 로고    scopus 로고
    • Gastrointestinal food allergy: new insights into pathophysiology and clinical perspectives
    • Bischoff, S. & Crowe, S.E. (2005). Gastrointestinal food allergy: new insights into pathophysiology and clinical perspectives. Gastroenterology, 128, 1089-1113.
    • (2005) Gastroenterology , vol.128 , pp. 1089-1113
    • Bischoff, S.1    Crowe, S.E.2
  • 7
    • 0034173371 scopus 로고    scopus 로고
    • Microwave-enhanced folding and denaturation of globular proteins
    • Bohr, H. & Bohr, J. (2000). Microwave-enhanced folding and denaturation of globular proteins. Physiology Review, E, 61, 4310-4314.
    • (2000) Physiology Review, E , vol.61 , pp. 4310-4314
    • Bohr, H.1    Bohr, J.2
  • 9
    • 0028950420 scopus 로고
    • Hydrolysis of beta-lactoglobulin by pepsin and thermolysin under high hydrostatic pressure
    • Dufour, E., Hervé, G. & Haertlé, T. (1995). Hydrolysis of beta-lactoglobulin by pepsin and thermolysin under high hydrostatic pressure. Biopolymers, 35, 475-483.
    • (1995) Biopolymers , vol.35 , pp. 475-483
    • Dufour, E.1    Hervé, G.2    Haertlé, T.3
  • 10
    • 80255127583 scopus 로고    scopus 로고
    • Combined microwave and enzymatic treatments for β-lactoglobulin and bovine whey proteins and their effect on the IgE immunoreactivity
    • El Mecherfi, K.E., Saidi, D., Kheroua, O. et al. (2011). Combined microwave and enzymatic treatments for β-lactoglobulin and bovine whey proteins and their effect on the IgE immunoreactivity. European Food Research and Technology, 233, 859-867.
    • (2011) European Food Research and Technology , vol.233 , pp. 859-867
    • El Mecherfi, K.E.1    Saidi, D.2    Kheroua, O.3
  • 11
    • 0037432668 scopus 로고    scopus 로고
    • Animal models in food allergy: assessment of allergenicity and preventive activity of infant formulas
    • Fritsché, R. (2003). Animal models in food allergy: assessment of allergenicity and preventive activity of infant formulas. Toxicology Letters, 140-141, 303-309.
    • (2003) Toxicology Letters , vol.140-141 , pp. 303-309
    • Fritsché, R.1
  • 12
    • 0015311097 scopus 로고
    • Ionic Conductances of Extracellular Shunt Pathway in Rabbit Ileum Influence of shunt on transmural sodium transport and electrical potential differences
    • Frizzell, R.A. & Schultz, S.G. (1972). Ionic Conductances of Extracellular Shunt Pathway in Rabbit Ileum Influence of shunt on transmural sodium transport and electrical potential differences. Journal of General Physiology, 59, 318-346.
    • (1972) Journal of General Physiology , vol.59 , pp. 318-346
    • Frizzell, R.A.1    Schultz, S.G.2
  • 13
    • 85028106797 scopus 로고    scopus 로고
    • Mutational analysis of major IgE-binding epitopes of recombinant bovine αS1-casein
    • Gaudin, J.C., Rabesona, H., Nioi, C. et al. (2011). Mutational analysis of major IgE-binding epitopes of recombinant bovine αS1-casein. Clinical and Translational Allergy, 1, 3.
    • (2011) Clinical and Translational Allergy , vol.1 , pp. 3
    • Gaudin, J.C.1    Rabesona, H.2    Nioi, C.3
  • 14
    • 84872142559 scopus 로고    scopus 로고
    • An investigation of the effect of microwave treatment on the structure and unfolding pathways of β-lactoglobulin using FTIR spectroscopy with the application of two-dimensional correlation spectroscopy (2D-COS)
    • Gomaa, A.I., Sedman, J. & Ismail, A.A. (2013). An investigation of the effect of microwave treatment on the structure and unfolding pathways of β-lactoglobulin using FTIR spectroscopy with the application of two-dimensional correlation spectroscopy (2D-COS). Vibrational Spectroscopy, 65, 101-109.
    • (2013) Vibrational Spectroscopy , vol.65 , pp. 101-109
    • Gomaa, A.I.1    Sedman, J.2    Ismail, A.A.3
  • 16
    • 33846027855 scopus 로고    scopus 로고
    • Microwave-assisted digestion of β-lactoglobulin by pronase, α-chymotrypsin and pepsin
    • Izquierdo, F., Inteaz, A., Varoujan, Y. & Gomez, R. (2007). Microwave-assisted digestion of β-lactoglobulin by pronase, α-chymotrypsin and pepsin. International Dairy Journal, 17, 465-470.
    • (2007) International Dairy Journal , vol.17 , pp. 465-470
    • Izquierdo, F.1    Inteaz, A.2    Varoujan, Y.3    Gomez, R.4
  • 17
    • 78649854606 scopus 로고    scopus 로고
    • High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens
    • Johnson, P.E., Van der Plancken, I., Balasa, A. et al. (2010). High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens. Molecular Nutrition & Food Research, 54, 1701-1710.
    • (2010) Molecular Nutrition & Food Research , vol.54 , pp. 1701-1710
    • Johnson, P.E.1    Van der Plancken, I.2    Balasa, A.3
  • 19
    • 33846785047 scopus 로고    scopus 로고
    • Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature
    • Kleber, N., Maier, S. & Hinrichs, J. (2007). Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature. Innovative Food Science & Emerging Technologies, 8, 39-45.
    • (2007) Innovative Food Science & Emerging Technologies , vol.8 , pp. 39-45
    • Kleber, N.1    Maier, S.2    Hinrichs, J.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0033942728 scopus 로고    scopus 로고
    • A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses
    • Li, X.M., Serebrisky, D., Lee, S.Y. et al. (2000). A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses. Journal of Allergy and Clinical Immunology, 106, 150-158.
    • (2000) Journal of Allergy and Clinical Immunology , vol.106 , pp. 150-158
    • Li, X.M.1    Serebrisky, D.2    Lee, S.Y.3
  • 23
    • 84987300635 scopus 로고
    • Preparation of β-lactoglobulin and p-lactoglobulin-free proteins from whey retentate by NaCI salting out at low pH
    • Mailliart, P. & Ribadeau-Dumas, B. (1988). Preparation of β-lactoglobulin and p-lactoglobulin-free proteins from whey retentate by NaCI salting out at low pH. Journal of Food Science, 53, 743-745.
    • (1988) Journal of Food Science , vol.53 , pp. 743-745
    • Mailliart, P.1    Ribadeau-Dumas, B.2
  • 24
    • 0027244732 scopus 로고
    • Intestinal epithelial function: the case for immunophysiological regulation
    • McKay, D.M. & Perdue, D.M.H. (1993). Intestinal epithelial function: the case for immunophysiological regulation. Digestive Diseases and Sciences, 38, 1377-1387.
    • (1993) Digestive Diseases and Sciences , vol.38 , pp. 1377-1387
    • McKay, D.M.1    Perdue, D.M.H.2
  • 25
    • 20744450734 scopus 로고    scopus 로고
    • Influence of thermal processing on the allergenicity of peanut proteins
    • Mondoulet, L., Paty, E., Drumare, M.F. et al. (2005). Influence of thermal processing on the allergenicity of peanut proteins. Journal of Agriculture and Food Chemistry, 53, 4547-4553.
    • (2005) Journal of Agriculture and Food Chemistry , vol.53 , pp. 4547-4553
    • Mondoulet, L.1    Paty, E.2    Drumare, M.F.3
  • 27
    • 30744443867 scopus 로고    scopus 로고
    • Development of probiotic cheddar cheese containing Lactobacillus acidophilus, Lb. casei, Lb. paracasei and Bifidobacterium spp. and the influence of these bacteria on proteolytic patterns and production of organic acid
    • Ong, L., Henriksson, A. & Shah, N.P. (2006). Development of probiotic cheddar cheese containing Lactobacillus acidophilus, Lb. casei, Lb. paracasei and Bifidobacterium spp. and the influence of these bacteria on proteolytic patterns and production of organic acid. International Dairy Journal, 16, 446-456.
    • (2006) International Dairy Journal , vol.16 , pp. 446-456
    • Ong, L.1    Henriksson, A.2    Shah, N.P.3
  • 28
    • 0036838857 scopus 로고    scopus 로고
    • Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: a new approach to protein digestion in minutes
    • Pramanik, B.N., Mirza, U.A., Ing, Y.H. et al. (2002). Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: a new approach to protein digestion in minutes. Protein Science, 11, 2676-2687.
    • (2002) Protein Science , vol.11 , pp. 2676-2687
    • Pramanik, B.N.1    Mirza, U.A.2    Ing, Y.H.3
  • 31
    • 79952489287 scopus 로고    scopus 로고
    • Thermal and nonthermal methods for food allergen control
    • Shriver, S.K. & Yang, W.W. (2011). Thermal and nonthermal methods for food allergen control. Food Engineering Review, 3, 26-43.
    • (2011) Food Engineering Review , vol.3 , pp. 26-43
    • Shriver, S.K.1    Yang, W.W.2
  • 33
    • 0002887986 scopus 로고    scopus 로고
    • Effect of microwaves on biological and chemical systems
    • Tong, C.H. (1996). Effect of microwaves on biological and chemical systems. Microwave World, 17, 14-23.
    • (1996) Microwave World , vol.17 , pp. 14-23
    • Tong, C.H.1
  • 34
    • 0028295255 scopus 로고
    • Increased intestinal sugar permeability after challenge in children with cow's milk allergy or intolerance
    • Troncone, R., Caputo, N., Florio, G. & Finelli, E. (1994). Increased intestinal sugar permeability after challenge in children with cow's milk allergy or intolerance. Allergy, 49, 142-146.
    • (1994) Allergy , vol.49 , pp. 142-146
    • Troncone, R.1    Caputo, N.2    Florio, G.3    Finelli, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.