Phospholipid/fatty acid-induced secondary structural change in β- lactoglobulin during heat-induced gelation

Journal of Agricultural and Food Chemistry

Volumn 48, Issue 3, 2000, Pages 605-610

  Ikeda, Shinya ^a   Foegeding, E Allen ^a   Hardin, Charles C ^a  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Lactoglobulin; Fatty acid; Gelation; Phosphatidylcholine; Secondary structure; Viscoelasticity

Indexed keywords

BETA LACTOGLOBULIN; BUTYRIC ACID; FATTY ACID; LACTOGLOBULIN; MILK; OLEIC ACID; PALMITIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; GEL; HEAT; HEATING; HUMAN; OSCILLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; VISCOELASTICITY;

FATTY ACIDS; GELS; HEAT; HUMANS; LACTOGLOBULINS; PHOSPHATIDYLCHOLINES; PROTEIN STRUCTURE, SECONDARY;

EID: 0034073314     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf990434h     Document Type: Article

References (40)

1. Bell, K.; McKenzie, H. A. The isolation and properties of bovine β-lactoglobulin C. Biochim. Biophys. Acta 1967, 147, 109-122.
2. 1H NMR study. J. Agric. Food Chem. 1998, 46, 1805-1813.
3. Ben-Tal, N.; Honig, B.; Miller, C.; McLaughlin, S. Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles. Biophys. J. 1997, 73, 1717-1727.
4. Bowland, E. L.; Foegeding, E. A.; Hamann, D. Rheological analysis of anion-induced matrix transformations in thermally induced whey protein isolate gels. Food Hydrocolloids 1995, 9, 57-64.
5. Brown, E. M.; Carroll, R. J.; Pfeffer, P. E.; Sampugna, J. Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidylcholine. Lipids 1983, 18, 111-118.
6. Chen, S. X.; Hardin, C. C.; Swaisgood, H. E. Purification and characterization of β-structural domains of β-lactoglobulin liberated by limited proteolysis. J. Protein Chem. 1993, 12, 613-625.
7. Chen, Y.; Shapira, R.; Eisenstein, M.; Montville, T. J. Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure. Appl. Environ. Microbiol. 1997, 63, 524-531.
8. Clark, A. H.; Judge, F. J.; Richards, J. B.; Stubbs, J. M.; Suggett, A. Electron microscopy of network structures in thermally induced globular protein gel. Int. J. Pept. Protein Res. 1981a, 17, 380-392.
9. Clark, A. H.; Saunderson, D. H. P.; Suggett, A. Infrared and laser-Raman spectroscopic studies of thermally induced globular protein gels. Int. J. Pept. Protein Res. 1981b, 17, 353-364.
10. Compton, L. A.; Johnson, W. C., Jr. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 1986, 155, 155-167.
11. Cornell, D. G.; Patterson, D. L. Interaction of phospholipids in monolayers with β-lactoglobulin absorbed from solution. J. Agric. Food Chem. 1989, 37, 1455-1459.
12. Creamer, L. K.; MacGibbon, A. K. H. Some recent advances in the basic chemistry of milk proteins and lipids. Int. Dairy J. 1996, 6, 539-568.
13. Denisov, G.; Wanaski, S.; Luan, P.; Glaser, M.; McLaughlin, S. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phospatidylserine and phosphatidylinositol 4,5-bisphosphate: An electrostatic model and experimental results. Biophys. J. 1998, 74, 731-744.
14. Foegeding, E. A.; Kuhn, P. R.; Hardin, C. C. Specific divalent cation induced changes during gelation of β-lactoglobulin. J. Agric. Food Chem. 1992, 40, 2092-2097.
15. Foegeding, E. A.; Bowland, E. L.; Hardin, C. C. Factors that determine the fracture properties and microstructure of globular protein gels. Food Hydrocolloids 1995, 9, 237-249.
16. Frapin, D.; Dufour, E.; Haertle, T. Probing the fatty acid binding site of β-lactoglobulins. J. Protein Chem. 1993, 12, 443-449.
17. Griffin, W. G.; Griffin, M. C. A., Martin, S. R., Price, J. Molecular basis of thermal aggregation of bovine β-lactoglobulin A. J. Chem. Soc., Faraday Trans. 1993, 89, 3395-3406.
18. Hagiwara, T.; Kumagai, H.; Nakamura, K. Fractal analysis of aggregates formed by heating dilute BSA solutions using light scattering methods. Biosci. Biotech. Biochem. 1996, 60, 1757-1763.
19. Hines, M. E.; Foegeding, E. A. Interactions of α-lactalbumin and bovine serum albumin with β-lactoglobulin in thermally induced gelation. J. Agric. Food Chem. 1993, 41, 341-346.
20. Ikeda, S.; Foegeding, E. A. Effects of lecithin on thermally induced whey protein isolate gels. Food Hydrocolloids 1999a, 13, 239-244.
21. Ikeda, S.; Foegeding, E. A. Dynamic viscoelastic properties of thermally induced whey protein isolate gels with added lecithin. Food Hydrocolloids 1999b, 13, 245-254.
22. Ikeda, S.; Foegeding, E. A.; Hagiwara, T. Rheological study on fractal nature of protein gel structure. Langmuir 1999, 15, 8584-8589.
23. Johnson, W. C., Jr. Secondary structure of proteins through circular dichroism spectroscopy. Annu. Rev. Biophys. Biophys. Chem. 1988, 17, 145-166.
24. Johnson, W. C., Jr. Protein secondary structure and circular dichroism: A practical guide. Proteins 1990, 7, 205-214.
25. Li, H.; Hardin, C. C.; Foegeding, E. A. NMR studies of thermal denaturation and cation-mediated aggregation of β-lactoglobulin. J. Agric. Food Chem. 1994, 42, 2411-2420.
26. Matsuura, J. E.; Manning, M. C. Heat-Induced gel formation of β-lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy. J. Agric. Food Chem. 1984, 42, 1650-1656.
27. McBain, J. W.; Sierichs, W. C. The solubility of sodium and potassium soaps and the phase diagrams of aqueous potassium soaps. J. Am. Chem. Soc. 1948, 25, 221-225.
28. McBain, J. W.; Vold, R. D.; Gardiner, K. Phase boundaries in ternary systems of sodium oleate, compared with other soaps. Oil Soap 1943, 20, 221-223.
29. Morr, C. V.; Foegeding, E. A. Composition and functionality of commercial whey and milk protein concentrates and isolates: A status report. Food Technol. 1990, 44, 100-112.
30. Papiz, M. Z.; Sawyer, L.; Eliopoulos, E. E.; North, A. C. T.; Findlay, J. B. C.; Sivaprasadarao, R.; Jones, T. A.; Newcomer, M. E.; Kraulis, P. J. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 1986, 324, 383-385.
31. Pedersen, A. O.; Mensberg, K-L. D.; Kragh-Hansen, U. Effects of ionic strength and pH on the binding of medium-chain fatty acids to human serum albumin. Eur. J. Biochem. 1995, 233, 395-405.
32. Qi, X. L.; Holt, C.; McNulty, D.; Clarke, D. T.; Brownlow, S.; Jones, G. R. Effect of temperature on the secondary structure of β-lactoglogulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem. J. 1997, 324, 341-346.
33. Shimizu, M.; Saito, M. Lipid-protein interaction at an emulsified oil surface: Protein structures and their roles in lipid binding. ACS Symp. Ser. 1996, 650, 156-165.
34. Spector, A. A.; Fletcher, J. E. Binding of long chain fatty acids to β-lactoglobulin. Lipids 1970, 5, 403-411.
35. Terzi, E.; Hölzemann, G.; Seelig, J. Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes. Biochemistry 1997, 36, 14845-14852.
36. van Vliet, T. Rheological properties of filled gels. Influence of filler matrix interaction. Colloid Polym. Sci. 1988, 266, 518-524.
37. Vaghela, M.; Kilara, A. Lipid composition of whey protein concentrates manufactured commercially and in the laboratory. J. Dairy Sci. 1996, 79, 1172-1183.
38. Wang, Q.; Allen, J. C.; Swaisgood, H. E. Protein concentration dependence of palmitate binding to β-lactoglobulin. J. Dairy Sci. 1998, 81, 76-81.
39. Yuno-Ohta, N.; Higasa, T.; Tatsumi, E.; Sakurai, H.; Asano, R.; Hirose, M. Formation of fatty acid salt-induced gel of ovalbumin and the mechanism for gelation. J. Agric. Food Chem. 1998, 46, 4518-4523.
40. Ziegler, G. R.; Foegeding, E. A. The gelation of proteins. Adv. Food Nutr. Res. 1990, 34, 203-298.