Abstract
Proton and deuterium NMR relaxation methods were used to characterize water compartmentalization and hydration in work-free wheat flour doughs. Transverse (spin-spin) relaxation measurements define three motionally unique water compartments in the work-free dough preparations. The apparent occupancy fraction and relative mobility of each water domain are found to be functions of moisture content, temperature, and flour type. Additionally, the number of relaxation-resolved water compartments and their characteristic relaxation rate constants are found to depend critically on both moisture content and the interpulse-delay employed for the multi-pulse relaxation experiments. Under controlled experimental conditions, dynamics between the three water compartments can be observed to be consistent with the onset of flour hydration. The most notable observation during the initial period of hydration is a loss of “free” or “loosely bound” water to environments characterized by less mobility. Freezing studies show that hard wheat doughs have slightly less amorphous, non-freezable water than do soft wheat flour doughs prepared under similar conditions.
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References
A.H. Bloksma, Flour composition, dough rheology, and baking quality, Cereal Sci. Today 17:380 (1972).
S.J. Richardson, I.C. Baianu, and M.P. Steinberg, Mobility of water in wheat flour suspensions as studied by proton and oxygen-17 nuclear magnetic resonance, J. Agric. Food Chem. 34:17 (1986).
J.L. Finney, J.M. Goodfellow, and P.L. Poole, The structure and dynamics of water in globular proteins, in: “Structural Molecular Biology,” D.B. Davies, W. Saenger, and S.S. Danyluk, eds., Plenum Press, New York (1982).
P.S. Belton, R.R. Jackson, and K.J. Packer, Pulsed NMR studies of water in striated muscle: transverse nuclear spin relaxation times and freezing effects, Biochem. Biophys. Acta. 286:16 (1972).
H.A. Resing, A.N. Garroway, and K.R. Foster, Bounds on bound water: transverse and rotating frame NMR relaxation in muscle tissue, in: “Magnetic Resonance in Colloid and Interface Science,” H.A. Resing and C.G. Wade, eds., American Chemical Society, Washington, DC (1976).
H.K. Leung and M.P. Steinberg, Water binding of food constituents as determined by NMR, freezing, sorption, and dehydration, J. Food Sci. 44:1212 (1979).
H.K. Leung, J.A. Magnuson, and B.L. Bruinsma, Pulsed nuclear magnetic resonance study of water mobility in flour doughs, J. Food Sci. 44:1408 (1979).
H.K. Leung, J.A. Magnuson, and B.L. Bruinsma, Pulsed nuclear magnetic resonance study of water mobility in flour doughs, J. Food Sci. 48:45 (1983).
J.R. Zimmerman and W.E. Brittan, NMR studies in multiple phase systems: lifetime of a water molecule in an absorbing phase on silica gel, J. Phvs. Chem. 61:1328 (1957).
H.A. Resing, Nuclear magnetic resonance relaxation of molecules adsorbed on surfaces, Adv. Mol. Relaxation Processes 3:199 (1968).
S.H. Koenig, K. Hallenga, and M. Shporer, Protein-water interaction studied by solvent 1H, 2H, and 17O magnetic resonance, Proc. Nat. Acad. Sci. 72:2667 (1975).
S.H. Koenig, The dynamics of water-protein interactions: results from measurements of nuclear magnetic relaxation dispersion, in: “Water in Polymers,” S.P. Rowland, ed., Amer. Chem. Soc, Washington, DC (1980).
R.G. Bryant, NMR relaxation studies of solute-solvent interactions, Ann. Rev. Phvs. Chem. 29:167 (1978).
R.G. Bryant, Water-protein interactions: NMR results on hydrated lysozyme, Biophvs. J. 32:80 (1980).
G.D. Fullerton, V.A. Ord, and I.L. Cameron, An evaluation of the hydration of lysozyme by an NMR titration method, Biochem. Biophys. Acta. 869:230 (1986).
K.B. Lange, G.D. Fullerton, and I.L. Cameron, Experimental confirmation of full molecular hydration, Seventh Annual Meeting of Society of Magnetic Resonance in Medicine, San Francisco (1988).
P.J. Lillford, A.H. Clark, and D.V. Jones, Distribution of water in heterogeneous food and model systems, in: “Water in Polymers,” S.P. Rowland, ed., American Chemical Society, Washington, DC (1980).
S. Meiboom and P. Gill, Measuring nuclear relaxation time, Rev. Sci. Instr. 29:688 (1958).
G.L. Bretthorst, Baysian spectrum analysis and parameter estimation, in: “Lecture Notes and Statistics,” Vol. 48, Springer-Verlag, New York, (1988).
J.S. Leigh, Jr., Relaxation times in systems with chemical exchange: some exact solutions, J. Magn. Res. 4:308 (1971).
H.T. Edzes and E.T. Samalski, Cross relaxation and spin diffusion in the proton NMR of hydrated collagen, Nature (London) 265:521 (1977).
S.H. Koenig, R.G. Bryant, K. Halenga, and G.S. Jacob, Magnetic cross-relaxation among protons in protein solutions, Biochemistry 17:4348 (1978).
R.G. Bryant and W.M. Shirley, Water-protein interactions, in: “Water in Polymers,” S.P. Rowland, ed., American Chemical Society, Washington, DC (1980).
W. Bushuk and V.K. Mehrotra, Studies of water binding by differential thermal analysis. II: dough studies using the boiling mode, Cereal Chem. 54:311 (1977).
E.L. Hahn, Spin echoes, Phys. Rev. 80:580 (1950).
H.Y. Carr and E.M. Purcell, Effects of diffusion on free precession in nuclear magnetic resonance experiments, Phys. Rev. 94:630 (1954).
Z. Luz and S. Meiboom, Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution, J. Chem. Phys. 39:366 (1963).
G.E. Santyr, R.M. Honkelman, and M.J. Bronskill, Variation in measured transverse relaxation in tissue resulting from spin-locking with the CPMG sequence, J. Magn. Res. 79:28 (1988).
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d’Avignon, D.A., Hung, CC., Pagel, M.T.L., Hart, B., Bretthorst, G.L., Ackerman, J.J.H. (1991). 1H and 2H NMR Studies of Water in Work-Free Wheat Flour Doughs. In: Levine, H., Slade, L. (eds) Water Relationships in Foods. Advances in Experimental Medicine and Biology, vol 302. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0664-9_26
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DOI: https://doi.org/10.1007/978-1-4899-0664-9_26
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