Molecular Dynamics of Water in Foods and Related Model Systems: Multinuclear Spin Relaxation Studies and Comparison with Theoretical Calculations

Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 302)


A review of recent studies of molecular dynamics of water in foods and model systems is presented, and the theoretical results are compared with experimental data obtained by several techniques. Both theoretical and experimental approaches are discussed for electrolytes, carbohydrates, and food proteins in solution. Theoretical results from Monte Carlo simulations are compared with experimental NMR relaxation data for quadrupolar nuclei such as those of deuterium and oxygen-17.

Hydration studies of wheat, soybean, corn, and myofibrillar proteins by multinuclear spin relaxation techniques are discussed, and several new approaches to the analysis of the experimental data are considered. Correlation times of water motions in hydrated food systems are determined from NMR and dielectric relaxation data. The values of the correlation times for dilute solutions of electrolytes and carbohydrates estimated by NMR are in good agreement with those calculated from dielectric relaxation data, but seem to differ significantly from those proposed from Monte Carlo simulations. Several new and important results concerning the hydration of potato and cereal starches are presented, showing the very different hydration behaviors of these two major groups of starches. The combination of molecular dynamics computations with NMR relaxation techniques will hopefully stimulate novel technological developments in food engineering based on such fundamental studies.


Potato Starch Myofibrillar Protein Nuclear Magnetic Resonance Relaxation Nuclear Magnetic Resonance Peak Wheat Gliadin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    L.V. Woodcock, Model of the instantaneous structure of a liquid, Nature 232:63 (1971).Google Scholar
  2. 2.
    S. Engstrom, B. Johnson, and B. Jonsson, A molecular approach to quadrupole relaxation. Monte Carlo simulations of dilute Li+, Na+ and Cl aqueous solutions, J. Magn. Reson. 50:1 (1982).Google Scholar
  3. 3.
    H.G. Hertz, Magnetic relaxation by quadrupole introduction of ionic nuclei in electrolyte solutions, Ber. Bunsenges. Phys. Chem. 77:531 and 688 (1973).Google Scholar
  4. 4.
    H. Holz, G. Keller, H. Hersmold, and C. Yoon, Nuclear magnetic relaxation of alkali metal ions in aqueous solutions, Ber. Bunsenges. Phys. Chem. 78:493 (1974).Google Scholar
  5. 5.
    K.A. Valiev and H. Khabibullin, Nuclear magnetic resonance and the structure of aqueous electrolyte solutions, Russ. J. Phys. Chem. 35:1118 (1961).Google Scholar
  6. 6.
    J.T. Hynes and P.G. Wolynes, A continuum theory for quadrupole relaxation of ions in solution, J. Chem. Phys. 75:395 (1981).CrossRefGoogle Scholar
  7. 7.
    C. Deverell, Nuclear magnetic shielding of hydrated alkali and halide ions in aqueous solutions. Mol. Phys. 16:491 (1969).CrossRefGoogle Scholar
  8. 8.
    C. Clement and H. Popkie, Study of the structure of molecular complexes. 1. Energy surface of a water molecule in the field of a lithium positive ion, J. Chem. Phys. 57:1077 (1972).CrossRefGoogle Scholar
  9. 9.
    R.M. Lawrence and R.F. Kruh, X-ray diffraction studies of aqueous alkali-metal halide solutions, J. Chem. Phys. 47:4758 (1967).CrossRefGoogle Scholar
  10. 10.
    A.H. Narten, F. Vaslow, and H.A. Levy, Diffraction pattern and structure of aqueous lithium chloride solutions, J. Chem. Phys. 58:5017 (1973).CrossRefGoogle Scholar
  11. 11.
    G. Licheri, G. Piccaluga, and G. Pinna, X-ray diffraction studies of LiCl solutions, J. Appl. Cryst. 6:392 (1973).CrossRefGoogle Scholar
  12. 12.
    J.E. Enderby and G.W. Neilson, Structure of ionic solutions, Phys. Bull. 29:360 (1978).Google Scholar
  13. 13.
    J.E. Enderby and G.W. Neilson, Neutron scattering studies of ionic solutions, Adv. Phys. 29:323 (1980).CrossRefGoogle Scholar
  14. 14.
    I.C. Baianu, N. Boden, and M. Mortimer, A new approach to the structure of concentrated aqueous electrolyte solutions using pulsed NMR methods, Chem. Phvs. Letts. 54:169 (1978).CrossRefGoogle Scholar
  15. 15.
    R.M. Sternheimer, On nuclear quadrupole moments, Phys. Rev. 84:244 (1951).CrossRefGoogle Scholar
  16. 16.
    K.D. Sen and P.T. Narashimhan, Polarizabilities and antishielding factors in crystals, in: “Advances in Nuclear Quadrupole Resonance,” Vol. 1, J.A.S. Smith, ed., Heyden, London (1974).Google Scholar
  17. 17.
    I.C. Baianu and T.F. Kumosinski, Comparisons of local structure in aqueous solutions and glasses of lithium chloride, Chem. Phys. Letts. submitted (1990).Google Scholar
  18. 18.
    T.F. Kumosinski, T. Lioutas, and I.C. Baianu, Multinuclear spin relaxation and molecular dynamics of concentrated electrolyte solutions, J. Magn. Reson. submitted (1990).Google Scholar
  19. 19.
    N. Boden and M. Mortimer, Reorientation of D2O in concentrated aqueous solutions of lithium chloride studied by nuclear magnetic relaxation, J. Chem. Soc. Faraday Trans. II 74:354 (1978).CrossRefGoogle Scholar
  20. 20.
    H.L. Friedman, Introduction to general discussion, Disc. Faraday Chem. Soc., Ion-Ion and Ion-Solvent Interactions, 401 (1977).Google Scholar
  21. 21.
    F. Franks, D.S. Reid, and A. Suggett, Conformation and hydration of sugars and related compounds in dilute aqueous solution, J. Solution Chem. 2:99 (1973).CrossRefGoogle Scholar
  22. 22.
    L. Slade and H. Levine, Non-equilibrium behavior of small carbohydratewater systems, Pure Appl. Chem. 60:1841 (1988).CrossRefGoogle Scholar
  23. 23.
    A. Mora and I.C. Baianu, Hydration studies of maltodextrins by proton, deuterium and oxygen-17 nuclear magnetic resonance, J. Food Sci. 55:462 (1990).CrossRefGoogle Scholar
  24. 24.
    A. Mora and I.C. Baianu, 1H NMR and viscosity measurements on suspensions of carbohydrates from corn: the investigation of carbohydrate hydration and stereochemical effects in solution. Relationship to oxygen-17 and carbon-13 NMR data, J. Agric. Food Chem. 37:1459 (1989).CrossRefGoogle Scholar
  25. 25.
    F. Reuther, G. Damaschun, Ch. Gernat, F. Schierbaum, B. Kettlitz, S. Radosta, and A. Nothnagel, Molecular gelation mechanism of maltodextrins investigated by wide-angle X-ray scattering, J. Colloid Polym. Sci. 262:643 (1984).CrossRefGoogle Scholar
  26. 26.
    P. Ahlstrom, O. Teleman, B. Jonsson, and S. Forsen, Molecular-dynamics simulation of parvalbumin in aqueous solution, J. Am. Chem. Soc. 109:1541 (1987).CrossRefGoogle Scholar
  27. 27.
    A. Kalk and H.J.C. Berendsen, Proton magnetic relaxation and spin diffusion in proteins, J. Magn. Reson. 24:343 (1976).Google Scholar
  28. 28.
    H.T. Edzes and E.T. Samulski, The measurement of cross-relaxation effects in the proton NMR spin-lattice relaxation of water in biological systems: hydrated collagen and muscle, J. Magn. Reson. 31:207 (1978).Google Scholar
  29. 29.
    D. Lankhorst and J.C. Leyte, NMR relaxation study of hydrogen exchange in solutions of polyelectrolytes, Macromolecules 17:93 (1984).CrossRefGoogle Scholar
  30. 30.
    L. Piculell and B. Halle, Water spin relaxation in colloidal systems. 2. 0-17 and H-2 relaxation in protein solutions, J. Chem. Soc. Faraday Trans. 82:401 (1986).CrossRefGoogle Scholar
  31. 31.
    L. Piculell and B. Halle, Water spin relaxation in colloidal systems. 1. 0-17 and H-2 relaxation in dispersions of colloidal silica, J. Chem. Soc. Faraday. Trans. 182:387 (1986).Google Scholar
  32. 32.
    L. Kakalis and I.C. Baianu, Oxygen-17 and deuterium nuclear magnetic relaxation studies of lysozyme hydration in solution: field dispersion, concentration, pH/pD and protein activity dependences, Arch. Biochem. Biophvs. 267:829 (1988).CrossRefGoogle Scholar
  33. 33.
    S.H. Koenig, K. Hallenga, and M. Shporer, Protein-water interaction studied by solvent 1H, 2H and 170 magnetic relaxation, Proc. Natl. Acad. Sci. USA 72:2667 (1975).CrossRefGoogle Scholar
  34. 34.
    J.R. Zimmerman and W.E. Brittin, Nuclear magnetic resonance studies in multiple phase systems: life-times of water molecules in an adsorbing phase on silica gel, J. Phys. Chem. 61:1328 (1957).CrossRefGoogle Scholar
  35. 35.
    E. Gratton, J.R. Alcala, and G. Marriott, Rotations of tryptophan residues in proteins, Biochem. Soc. Trans. 14:835 (1986).Google Scholar
  36. 36.
    T.S. Lioutas, I.C. Baianu, and M.P. Steinberg, Oxygen-17 and deuterium NMR studies of lysozyme hydration, Arch. Biochem. Biophys. 247:68 (1986).CrossRefGoogle Scholar
  37. T.S. Lioutas, I.C. Baianu, and M.P. Steinberg, J. Agric. Food Chem. 35:133 (1987).CrossRefGoogle Scholar
  38. 37.
    I.C. Baianu, H.S. Gutowsky, and E. Oldfield, Origin and behavior of deuteron spin echoes in selectively labeled amino acids, myoglobin microcrystals and purple membranes, Biochem. 23:3105 (1984).CrossRefGoogle Scholar
  39. 38.
    E. Oldfield and T.M. Rothgeb, NMR of individual sites in protein crystals. Magnetic ordering effects, J. Amer. Chem. Soc. 102:3635 (1980).CrossRefGoogle Scholar
  40. 39.
    T.M. Rothgeb and E. Oldfield, Nuclear magnetic resonance of heme protein crystals, J. Biol. Chem. 256:1432 (1981).Google Scholar
  41. 40.
    A. Mora, I.C. Baianu and P.J. Bechtel, Self-association and hydration of myosin A and B derived from 170 NMR measurements and a thermodynamic linkage approach, Biophys. J. 57:418a (1989).Google Scholar
  42. 41.
    A. Mora, I.C. Baianu, and P.J. Bechtel, The effects of salts, pH and protein-protein interactions on myosin hydration and aggregation state as determined by 1H NMR: a thermodynamic linkage analysis, submitted (1990).Google Scholar
  43. 42.
    T.F. Kumosinski, The use of thermodynamic linkage to study the saltinduced solubility change of soybean isolate, J. Agric. Food Chem. 36:110 (1988).CrossRefGoogle Scholar
  44. 43.
    T.A. Lioutas, I.C. Baianu, P.J. Bechtel, and M.P. Steinberg, Oxygen-17 and sodium-23 nuclear magnetic resonance studies of myofibrillar protein interactions with water and electrolytes in relation to sorption isotherms, J. Agric. Food Chem. 36:437 (1988).CrossRefGoogle Scholar
  45. 44.
    W.F. Harrington and M.E. Rodgers, Myosin, Ann. Rev. Biochem. 53:35 (1984).CrossRefGoogle Scholar
  46. 45.
    C.H. Ernes and A.J. Rowe, Hydrodynamics studies of the self association of vertebrate skeletal muscle myosin, Biochem. Biophys. Acta. 537:110 (1978).CrossRefGoogle Scholar
  47. 46.
    I.C. Baianu, High-resolution NMR of food proteins, in: “NMR in Agriculture,” P. Pfeffer and W. Gerasimowics, eds., CRC Press, Boca Raton, Florida (1989).Google Scholar
  48. 47.
    I.C. Baianu et al., Multinuclear spin relaxation studies of food proteins, agriculturally-important materials and related model systems, in: “NMR in Agriculture and Food Chemistry,” J. Finley, ed., Plenum Press, New York (1990).Google Scholar
  49. 48.
    J.D. Schofield and I.C. Baianu, Solid-state, cross-polarization magic-angle spinning carbon-13 NMR and biochemical characterization of wheat proteins, Cereal Chem. 59:240 (1982).Google Scholar
  50. 49.
    I.C. Baianu and H. Förster, Cross-polarization, high-field carbon-13 NMR techniques for studying physicochemical properties of wheat grain, flour, starch, gluten and wheat protein powders, J. Appl. Biochem. 2:347 (1980).Google Scholar
  51. 50.
    I.C. Baianu, Carbon-13 and proton NMR studies of wheat proteins, J. Sci. Food Agric. 32:309 (1981).CrossRefGoogle Scholar
  52. 51.
    I.C. Baianu, L.F. Johnson, and D.K. Waddell, High-resolution, proton, carbon-13 and nitrogen-15 NMR studies of wheat proteins at high magnetic fields: spectral assignments, changes in conformation with heat treatments of Flinor gliadins in solution. Comparison with gluten spectra, J. Sci. Food Agric. 33:373 (1982).CrossRefGoogle Scholar
  53. 52.
    I.C. Baianu, C. Gabrielle and R. Sheppard, unpublished results.Google Scholar
  54. 53.
    H.K. Leung, J.A. Magnuson, and B.L. Bruinsraa, Water binding of wheat flour doughs and breads as studied by deuteron relaxation, J. Food Sci. 48:95 (1983).CrossRefGoogle Scholar
  55. 54.
    L-J. Lo, V.A. White, and P. Chinachotti, Effect of sucrose on water binding behavior of wheat gluten as determined by 2H, 170 and 13C NMR, J. Food Sci. in press (1990).Google Scholar
  56. 55.
    S.J. Richardson, I.C. Baianu, and M.P. Steinberg, Relation between oxygen-17 NMR and rheological characteristics of wheat flour suspensions, J. Food Sci. 50:1148 (1985).CrossRefGoogle Scholar
  57. 56.
    I.C. Baianu, Solid-state NMR of food proteins, in: “Proc. ACS Symp. Solid State NMR in Agriculture,” Washington, D.C. (1983).Google Scholar
  58. 57.
    A. Mora and I.C. Baianu, Ion binding and hydration of wheat gliadins in solution with a paramagnetic, Mn+2 ion probe, submitted (1990).Google Scholar
  59. 58.
    A. Mora and I.C. Baianu, Interactions of wheat gliadins in solutions with carbohydrates, submitted (1990).Google Scholar
  60. 59.
    M.E. Augustine and I.C. Baianu, Basic studies of corn proteins for improved solubility and future utilization: a physicochemical approach, J. Food Sci. 52:649 (1987).CrossRefGoogle Scholar
  61. 60.
    P.A. Myers-Betts and I.C. Baianu, 1H NMR relaxation studies of corn protein activity in aqueous solutions, in: “Proceed. — Conf. Biotechnol. Res. Dir. Biomolecules,” Argonne Natl. Lab., Chicago, IL (1988).Google Scholar
  62. 61.
    P.A. Myers-Betts and I.C. Baianu, Determination of virial coefficients of corn zeins in alkaline solutions form 1H NMR relaxation measurements, J. Agric. Food Chem. 38:477 (1990).CrossRefGoogle Scholar
  63. 62.
    M.E. Augustine and I.C. Baianu, High resolution carbon-13 NMR of maize proteins, J. Cereal Sci. 4:371 (1986).CrossRefGoogle Scholar
  64. 63.
    J. Wyman, Jr., Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19:223 (1964).CrossRefGoogle Scholar
  65. 64.
    H.M. Farrell and T.F. Kumosinski, Modeling of calcium-induced solubility profiles of casein for biotechnology: influence of primary structure and post-translational modification, J. Ind. Microbiol. 3:25 (1988).CrossRefGoogle Scholar
  66. 65.
    T.F. Kumosinski, The use of thermodynamic linkage and non-linear regression analysis for studying protein interactions, in: “Advances in Food and Nutrition Research,” J. Kinsella, ed. (1990).Google Scholar
  67. 66.
    W. Melander and C. Horvath, Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series, Arch. Biochem. Biophys. 183:200 (1977).CrossRefGoogle Scholar
  68. 67.
    J.L. Shen, Solubility and viscosity, fundamental physicochemical and functional properties of isolated soy proteins, in: “Protein Functionality in Foods,” J.P. Cherry, ed., ACS Symposium Series 147, American Chemical Society, Washington, D.C. (1981).Google Scholar
  69. 68.
    L. Kakalis, I.C. Baianu, and T.F. Kumosinski, Oxygen-17 and deuterium NMR studies of soy protein hydration, J. Agric. Food Chem. in press (1990).Google Scholar
  70. 69.
    L. Kakalis, I.C. Baianu, Carbon-13 NMR of soy glycinin in D2O, J. Agric. Food Chem. 37:1222 (1989).CrossRefGoogle Scholar
  71. 70.
    A. Mora, T.F. Kumosinski, I.C. Baianu, and P.J. Bechtel, Self-association of myofibrillar proteins as determined by oxygen-17 NMR, submitted (1990).Google Scholar
  72. 71.
    T.H. Lechert, Water binding on starch: nuclear magnetic resonance studies on native and gelatinized starch, in: “Water Activity: Influences on Food Quality,” L.B. Rockland and G.F. Stewart, eds., Academic Press, New York (1981).Google Scholar
  73. 72.
    P.H. Yakubu, I.C. Baianu, and P.H. Orr, Unique hydration properties of potato starch determined by deuterium NMR, J. Food Sci. 55:458 (1990).CrossRefGoogle Scholar
  74. 73.
    P.H. Yakubu, I.C. Baianu, and P.H. Orr, Deuterium NMR studies of potato starch hydration, in: this book.Google Scholar
  75. 74.
    S.J. Richardson, I.C. Baianu, and M.P. Steinberg, Mobility of water in corn starch suspensions determined by nuclear magnetic resonance, Starch 39:79 (1987).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  1. 1.University of Illinois at UrbanaUrbanaUSA
  2. 2.Agricultural and Food Chemistry NMR FacilityUrbanaUSA
  3. 3.Muscle Biology LaboratoryUrbanaUSA
  4. 4.USDA Eastern Regional Research CenterPhiladelphiaUSA

Personalised recommendations