Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels

Food Hydrocolloids

Volumn 18, Issue 3, 2004, Pages 489-498

  Ikeda, Shinya ^a   Li Chan, Eunice C Y ^b  

^a Osaka Prefecture University   (Japan)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Aggregation; Denaturation; Heat induced gelation; Raman spectroscopy; Lactoglobulin

Indexed keywords

AMINO ACIDS; GELATION; GELS; HEAT RESISTANCE; HYDROGEN BONDS; HYDROPHOBICITY; SODIUM CHLORIDE;

HEAT-INDUCED GELATION; HYDROPHOBIC INTERACTIONS; LACTOGLOBULIN; MOLECULAR STRUCTURAL; PARTICULATES; RAMAN SCATTERING SPECTROSCOPY; SECONDARY STRUCTURES; TYROSINE RESIDUES; VIBRATIONAL BANDS; Β-LACTOGLOBULIN;

RAMAN SPECTROSCOPY;

AMINO ACID; BETA LACTOGLOBULIN; HYDROGEN; SODIUM CHLORIDE; TRYPTOPHAN; TYROSINE;

ALPHA HELIX; AMINO ACID ANALYSIS; ARTICLE; GEL; GELATION; HEAT; HEAT TOLERANCE; HEATING; HYDROGEN BOND; HYDROPHOBICITY; PH; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; STRUCTURE ANALYSIS; TEMPERATURE; TIME; VIBRATION;

EID: 1542299045     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2003.07.003     Document Type: Article

References (51)

1. Allain A.-F., Paquin P., Subirade M. Relationships between conformation of β-lactoglobulin in solution and gel states as revealed by attenuated total reflection Fourier transform infrared spectroscopy. International Journal of Biological Macromolecules. 26:1999;337-344.
2. Alting A.C., Hamer R.J., de Kruif C.G., Visschers R.W. Formation of disulfide bonds in acid-induced gels of preheated whey protein isolate. Journal of Agriculture and Food Chemistry. 48:2000;5001-5007.
3. Aymard P., Gimel J.C., Nicolai T., Durand D. Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH 7. Journal de Chimie Physique. 93:1996;987-997.
4. Aymard P., Nicolai T., Durand D. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules. 32:1999;2542-2552.
5. Bell K., McKenzie H.A. The isolation and properties of bovine β-lactoglobulin C. Biochimica et Biophysica Acta. 147:1967;109-122.
6. Bellocq A.M., Lord R.C., Mendelsohn R. Laser-excited Raman spectroscopy of biomolecules III. Native bovine serum albumin and β-lactoglobulin. Biochimica et Biophysica Acta. 257:1972;280-287.
7. 1H NMR study. Journal of Agricultural and Food Chemistry. 46:1998;1805-1813.
8. Blanch E.W., Hecht L., Barron L.D. New insight into the pH-dependent conformational changes in bovine β-lactoglobulin from Raman optical activity. Protein Science. 8:1999;1362-1367.
9. Brownlow S., Cabral J.H.M., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., North A.C.T., Sawyer L. Bovine β-lactoglobulin at 1.8 Å resolution - still an enigmatic lipocalin. Structure. 5:1997;481-495.
10. Byler D.M., Susi H., Farrel H.M. Jr. Laser-Raman spectra, sulphydryl groups, and conformation of the cysteine linkages of β-lactoglobulin. Biopolymers. 22:1983;2507-2511.
11. Carew E.B., Stanley H.E., Seidel J.C., Gergely J. Studies of myosin and its proteolytic fragments by laser Raman spectroscopy. Biophysical Journal. 44:1983;219-224.
12. Carey P.R., Fast P., Kaplan H., Pozsgav M. Molecular structure of the protein crystal from Bacillus thuringiensis: a Raman spectroscopic study. Biochimica Biophysica Acta. 872:1986;169-176.
13. Clark A.H. Gelation of globular proteins. Hill S.E., Ledward D.A., Mitchell J.R. Functional properties of food macromolecules. 2nd ed. 1998;77-142 Aspen Publishers, Gaithersburg.
14. 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. International Journal of Peptide and Protein Research. 17:1981;380-392.
15. Clark A.H., Saunderson D.H.P., Suggett A. Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. International Journal of Peptide and Protein Research. 17:1981;353-364.
16. Fogolari F., Ragona L., Zetta L., Romagnoli S., De Kruif K.G., Molinari H. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Letters. 436:1998;149-154.
17. Frushour B.G., Koenig J.L. Raman studies of the crystalline, solution, and alkaline-denatured states of β-lactoglobulin. Biopolymers. 14:1975;649-662.
18. Gimel J.-C., Durand D., Nicolai T. Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins. Macromolecules. 27:1994;583-589.
19. -1 in the Raman spectra of tryptophan and related compounds. Spectrachimica Acta. 42A:1986;307-312.
20. Hoffmann M.A.M., van Mil P.J.J.M. Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds. Journal of Agricultural and Food Chemistry. 45:1997;2942-2948.
21. Howell N., Li-Chan E. Elucidation of interactions of lysozyme with whey proteins by Raman spectroscopy. International Journal of Food Science and Technology. 31:1996;439-451.
22. Ikeda S., Foegeding E.A., Hagiwara T. Rheological study on the fractal nature of the protein gel structure. Langmuir. 15:1999;8584-8589.
23. Ikeda S., Morris V.J. Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules. 3:2002;382-389.
24. Ikeda S., Nishinari K., Foegeding E.A. Mechanical characterization of network formation during heat-induced gelation of whey protein dispersions. Biopolymers. 56:2001;109-118.
25. Kavanagh G.M., Clark A.H., Ross-Murphy S.B. Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH β-lactoglobulin gels. International Journal of Biological Macromolecules. 28:2000;41-50.
26. Kitagawa T., Azuma T., Hamaguchi K. The Raman spectra of Bence-Jones proteins. Disulfide stretching frequencies and dependence of Raman intensity of tryptophan residues on their environments. Biopolymers. 18:1979;451-465.
27. Koenig J.L., Frushour B.B. Raman scattering of chymotrypsinogen A, ribonuclease, and ovalbumin in the aqueous solution and solid state. Biopolymers. 11:1972;2505-2520.
28. Langton M., Hermansson A.-M. Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH. Food Hydrocolloids. 5:1992;523-539.
29. Lefevre T., Subirade M. Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels. Biopolymers. 54:2000;578-586.
30. Lefevre T., Subirade M. Molecular structure and interaction of biopolymers as viewed by Fourier transform infrared spectroscopy: model studies on β-lactoglobulin. Food Hydrocolloids. 15:2001;365-376.
31. Li-Chan E.C.Y. The applications of Raman spectroscopy in food science. Trends in Food Science and Technology. 7:1996;361-370.
32. Lin V.J.C., Koenig J.L. Raman studies of bovine serum albumin. Biopolymers. 15:1976;203-218.
33. Manderson G.A., Creamer L.K., Hardman M.J. Effect of heat treatment on the circular dichroism spectra of bovine β-lactoglobulin A, B, and C. Journal of Agricultural and Food Chemistry. 47:1999;4557-4567.
34. Manderson G.A., Hardman M.J., Creamer L.K. Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence. Journal of Agricultural and Food Chemistry. 47:1999;3617-3627.
35. Manderson G.A., Hardman M.J., Creamer L.K. Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C. Journal of Agricultural and Food Chemistry. 46:1998;5052-5061.
36. Miura T., Takeuchi H., Harada I. Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics. Biochemistry. 27:1988;88-94.
37. Molinari H., Ragona L., Varani L., Musco G., Consonni R., Zetta L., Monaco H.L. Partially folded structure of monomeric bovine β-lactoglobulin. FEBS Letters. 381:1996;237-243.
38. Nonaka M., Li-Chan E., Nakai S. Raman spectroscopic study of thermally induced gelation of whey proteins. Journal of Agricultural and Food Chemistry. 41:1993;1176-1181.
39. Ogawa M., Nakamura S., Horimoto Y., An H., Tsuchiya T., Nakai S. Raman spectroscopic study of changes in fish actomyosin during setting. Journal of Agricultural and Food Chemistry. 47:1999;3309-3318.
40. Panick G., Malessa R., Winter R. Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering. Biochemistry. 38:1999;6512-6519.
41. Qin B.Y., Bewley M.C., Creamer L.K., Baker E.N., Jameson G.B. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Science. 8:1999;75-83.
42. Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., Jameson G.B. Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry. 37:1998;14014-14023.
43. Qi X.L., Holt C., McNulty D., Clarke D.T., Brownlow S., Jones G.R. 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. Biochemical Journal. 324:1999;341-346.
44. Ragona L., Pusterla F., Zetta L., Monaco H., Molinari H.L. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Folding and Design. 2:1997;281-290.
45. Roefs S.P.F.M., De Kruif C.G. A model for the denaturation and aggregation of β-lactoglobulin. European Journal of Biochemistry. 226:1994;883-889.
46. -1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds. Biochemistry. 22:1975;4870-4876.
47. Stading M., Hermansson A.-M. Large deformation properties of β-lactoglobulin gel structures. Food Hydrocolloids. 5:1991;339-352.
48. Thomas G.J. Jr. Raman spectroscopy of protein and nucleic acid assemblies. Annual Review of Biophysics and Biomolecular Structure. 28:1999;1-27.
49. Tu A.T. Raman spectroscopy in biology: Principles and applications. 1982;Wiley, New York.
50. Van Dael H., Lafaut J.P., Van Cauwelaert F. Tyrosine group behaviour in bovine β-lactalbumin as revealed by its Raman effect. European Biophysics Journal. 14:1987;409-414.
51. Wen Z.Q., Hecht L., Barron L.D. β-Sheet and associated turn signatures in vibrational Raman optical activity spectra of proteins. Protein Science. 3:1994;435-439.