Physiological phosphatidylcholine protects bovine β-lactoglobulin from simulated gastrointestinal proteolysis

Molecular Nutrition and Food Research

Volumn 53, Issue SUPPL. 1, 2009, Pages

  Mandalari, Giuseppina ^a   Mackie, Alan M ^a   Rigby, Neil M ^a   Wickham, Martin S J ^a   Mills, E N Clare ^a  

^a NORWICH RESEARCH PARK   (United Kingdom)

Author keywords

Lactoglobulin; Food allergy; In vitro digestion; Phosphatidylcholine; Protein lipid interaction

Indexed keywords

LACTOGLOBULIN; PEPSIN A; PEPTIDE HYDROLASE; PHOSPHATIDYLCHOLINE;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; DIGESTION; DRUG EFFECT; ENZYMOLOGY; GASTROINTESTINAL TRACT; HEAT; METABOLISM; PROTEIN DENATURATION;

ANIMALS; CATTLE; DIGESTION; GASTROINTESTINAL TRACT; HOT TEMPERATURE; LACTOGLOBULINS; PEPSIN A; PEPTIDE HYDROLASES; PHOSPHATIDYLCHOLINES; PROTEIN DENATURATION;

BOVINAE;

EID: 67649909210     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.200800321     Document Type: Article

References (33)

1. Brownlow, S., Cabral, J. H. M., Cooper, R., Flower, D. F., et al., Bovine β-lactoglobulin at 1.8 resolution - still an enigmatic lipocalin, Structure 1997, 5, 481-495.
2. Kontopidis, G., Holt, C., Sawyer, L., The ligand-binding site of bovine beta-lactoglobulin: Evidence for a function? J. Mol. Biol. 2002, 318, 1043-1055.
3. Frapin, D., Dufour, E., Haertle, T., Probing the fatty acid binding site of beta-lactoglobulins, J. Protein Chem. 1993, 12,443-449.
4. Dufour, E., Genot, C., Haertle, T., beta-Lactoglobulin binding properties during its folding changes studied by fluorescence spectroscopy, Biochim. Biophys. Acta 1994, 1205, 105-112.
5. Qin, B. Y., Bewley, M. C., Creamer, L. K., Baker, H. M., et al., Structural basis of the Tanford transition of bovine beta-lactoglobulin, Biochemistry 1998, 37, 14014-14023.
6. Ragona, L., Fogolari, F., Catalano, M., Ugolini, R., et al., EF loop conformational change triggers ligand binding in beta-lactoglobulins, J. Biol. Chem. 2003, 278, 38840-38846.
7. Ragona, L., Fogolari, F., Zetta, L., Perez, M. D., et al., Bovine β-lactoglobulin: Interaction studies with palmitic acid, Prot. Sci. 2000, 9, 1347-1356.
8. Brown, E. M., Caroll, R. J., Pfeffer, P. E., Sampugna, J. J., Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidylcholine, Lipids 1983, 18, 111-118.
9. Lefevre, T., Subirade, M., Interaction of β-lactoglobulin with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy, Int. J. Biol. Macromol. 2000, 28, 59-67.
10. Cornell, D. G., Caroll, R. J., Miscibility in lipid-protein monolayers, J. Colloid Interface Sci. 1985, 108, 226-233.
11. Krinstensen, A., Nylander, T., Paulsson, M., Carlsson, A., Calorimetric studies of interactions between β-lactoglobulin and phospholipids in solutions, Int. Dairy J. 1997, 7, 87-92.
12. Lefevre, T., Subirade, M., Conformational rearrangements of β-lactoglobulin upon interaction with an anionic membrane, Biochim. Biophys. Acta 2001, 1549, 37-50.
13. Zhang, X., Keiderling, T. A., Lipid-induced conformational transitions of β-lactoglobulin, Biochemistry 2006, 45, 8444-8452.
14. Zhang, X., Ge, N., Keiderling, T. A., Electrostatic and hydrophobic interactions governing the interaction and binding of β-lactoglobulin to membranes, Biochemistry 2007, 46, 5252-5260.
15. Uhrinova, S., Smith, M. H., Jameson, G. B., Uhrín, D., et al., Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer, Biochemistry 2000, 4, 3565-3574.
16. Wal, J. M., Structure and function of milk allergens, Allergy 2001, 56, 35-38.
17. Mantyjarvi, R., Rautiainen, J., Virtanen, T., Lipocalins as allergens, Biochim. Biophys. Acta 2000, 1482, 308-317.
18. Jenkins, J. A., Breiteneder, H., Mills, E. C. N., Evolutionary distance from human homologs reflects allergenicity of animal food proteins, J. Allergy Clin. Immunol. 2007, 120, 1399-1405.
19. Mouecoucou, J., Villaume, C., S nchez, C., Mejean, L., Beta-lactoglobulin/polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of different Mr cutoffs, Biochim. Biophys. Acta 2004, 1670, 105-112.
20. Moreno, F. J., Mackie, A. R., Mills, E. C. N., Phospholipid interactions protect the milk allergen α-lactalbumin from proteolysis during in vitro digestion, J. Agric. Food Chem. 2005, 53,9810-9816.
21. Vassilopoulou, E., Rigby, N., Moreno, F. J., Zuidmeer, L., et al., Effect of in vitro gastric and duodenal digestion on the allergenicity of grape lipid transfer protein, J. Allergy Clin. Immunol. 2006, 118, 473-480.
22. Sreerma, N., Woody, R. W., A self-consistent method for the analysis of protein secondary structure from circular dichroism, Anal. Biochem. 1993, 209, 32-44.
23. Fu, T.-J., Abbott, U. R., Hatzos, C., Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid - a comparative study, J. Agric. Food Chem. 2002, 50, 7154-7160.
24. Schmidt, D. G., Meijer, R. J., Slangen, C. J., van Beresteijn, E. C., Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates, Clin. Exp. Allergy 1995, 25, 1007-1017.
25. Carey, M. C., Hernell, O., Digestion and absorption of fat, Semin. Gastrointest. Dis. 1992, 3, 189-208.
26. Qi, X. L., Brownlow, S., Holt, C., Sellers, P., Thermal denaturation of β-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05, Biochim. Biophys. Acta 1995, 1248, 43-49.
27. Iametti, S., De Gregori, B., Vecchio, G., Bonomi, F., Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin, Eur. J. Biochem. 1996, 237, 106-112.
28. Qi, X. L., Holt, C., McNulty, D., Clarke, D. T., et al., Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis, Biochem. J. 1997, 324, 341-346.
29. Maser, N. A., Benedek, G. A., Carey, M. C., Quasielastic light scattering of aqueous biliary lipid systems. Mixed micelle formation in bile salt-lecithin solutions, Biochemistry 1980, 19, 601-615.
30. Matsuoka, K., Maeda, M., Moroi, Y., Characteristics of con- jugate bile salt-phosphatidylcholine-cholesterol-water systems, Coll. Surf. 2004, 33, 101-109.
31. O'Neill, T. E., Kinsella, J. E., Binding of alkanone flavours to beta-lactoglobulin: Effects of conformational and chemical modification, J. Agric. Food Chem. 1987, 35, 770-774.
32. Sarker, D. K., Wilde, P. J., Clark, D. C., Competitive absorption of L-a-lysophosphatidylcholine/β-lactoglobulin mixtures at the interfaces of foams and foam lamellae, Coll. Surf. 1995, 3, 149-356.
33. Mendieta, J., Folqu, H., Tauler, R., Two-phase induction of the nonnative α-helical form of β-lactoglobulin in the presence of trifluoroethanol, Biophys. J. 1999, 76, 451-457.