Hostname: page-component-586b7cd67f-tf8b9 Total loading time: 0 Render date: 2024-11-26T21:29:41.759Z Has data issue: false hasContentIssue false
  • English
  • Français

Low-field nuclear magnetic resonance relaxation study of thermal effects on milk proteins

Published online by Cambridge University Press:  01 June 2009

Pierre Lambelet ,
Rafael Berrocal  and
Francine Renevey
Pierre Lambelet
Affiliation:
NESTEC Ltd, Nestlé Research Centre, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Suisse
Rafael Berrocal
Affiliation:
NESTEC Ltd, Nestlé Research Centre, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Suisse
Francine Renevey
Affiliation:
NESTEC Ltd, Nestlé Research Centre, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Suisse
Get access Rights & Permissions [Opens in a new window]

Summary

A recently described nuclear magnetic resonance (NMR) method was evaluated for its usefulness in studying thermal effects on milk proteins. The increase in water proton T2 relaxation rate observed during thermal treatment of aqueous whey protein solutions above the denaturing onset temperature paralleled results obtained with the standard Rowland (1938) method. The influence of milk constituants on NMR characteristics was analysed. The NMR response increased with the ionic strength and the addition of caseinate or casein micelles. The relevance of the T2 relaxation probe for studying thermal modifications of milk proteins is discussed. It is proposed to apply the NMR method for determining either reversible or irreversible thermal denaturation of whey proteins in model Systems.

Type
Original Articles
Information
Journal of Dairy Research , Volume 59 , Issue 4 , November 1992 , pp. 517 - 526
Copyright
Copyright © Proprietors of Journal of Dairy Research 1992

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Association of Official Analytical Chemists 1980 Official Methods of Analysis of the AOAC, 13th edn, Methods 16.047, 16.048 and 47.021 (Ed. Horwitz, W.). Washington, DC: AOACGoogle Scholar
Blicharska, B. & Rydzy, M. 1979 Investigation of protein denaturation by nuclear magnetic relaxation method. Acta Physica Polonica A56 439–443Google Scholar
Derbyshire, W. 1982 The dynamics of water in heterogeneous Systems with emphasis on subzero temperatures. In Water: a Comprehensive Treatise, vol. 7, pp 339–430 (Ed. Franks, F.). New York: Plenum PressGoogle Scholar
De Rham, O. & Chanton, S. 1984 Role of ionic environment in insolubilization of whey protein during heat treatment of whey products. Journal of Dairy Science 67 939–949CrossRefGoogle Scholar
De Wit, J. N. 1981 Structure and functional behaviour of whey proteins. Netherlands Milk and Dairy Journal 35 47–64Google Scholar
Donovan, M. & Mulvikill, D. M. 1987 Thermal denaturation and aggregation of whey proteins. Irish Journal of Food Science and Technology 11 87–100Google Scholar
Farrell, H. M., Pessen, H. & Kumosinski, T. F. 1989 Water interactions with bovine caseins by hydrogen-2 nuclear magnetic resonance relaxation studies: structural implications. Journal of Dairy Science 72 562–574CrossRefGoogle Scholar
Goldsmith, S. M. & Toledo, R. T. 1985 Studies on egg albumen gelation using nuclear magnetic resonance. Journal of Food Science 50 59–62CrossRefGoogle Scholar
Hills, B. P., Takacs, S. F. & Belton, P. S. 1990 A new interpretation of proton NMR relaxation time measurcmcnts of water in food. Food Chemistry 37 95–111.CrossRefGoogle Scholar
Kumosinski, T. F. & Pessen, H. 1982 A deutcron and proton magnetic resonance relaxation study of βlactoglobulin A association: some approaches to the Scatchard hydration of globular proteins. Archives of Biochemistry and Biophysics 218 286–302CrossRefGoogle Scholar
Kumosinski, T. F., Pessen, H., Prestrelski, S. J. & Farrell, H. M. 1987 Water interactions with varying molecular states of bovine casein: 2H NMR relaxation studies. Archives of Biochemistry and Biophysics 257 259–268CrossRefGoogle ScholarPubMed
Lambelet, P., Berrocal, R., Desarzens, C., Froehlicher, I. & Ducret, F. 1988 Pulsed low-resolution NMR investigations of protein sols and gels. Journal of Food Science 53 943–946, 964CrossRefGoogle Scholar
Lambelet, P., Berrocal, R. & Ducret, F. 1989 Low resolution NMR spectroscopy: a tool to study protein denaturation. I. Application to diamagnetic whey proteins. Journal of Dairy Research 56 211–222CrossRefGoogle Scholar
Lambelet, P., Ducret, F., Leuba, J. L. & Geoffroy, M. 1991 Low-field NMR relaxation study of the thermal denaturation of transferrins. Journal of Agricultural and Food Chemistry 39 287–292CrossRefGoogle Scholar
Mulvlhill, D. M. & Donovan, M. 1987 Whey proteins and their thermal denaturation – a review. Irish Journal of Food Science and Technology 11 43–75Google Scholar
Mulvihill, D. M. & Kinsella, J. E. 1988 Gelation of β-lactoglobulin: effects of sodium chloride and calcium chloride on the rheological and structural properties of gels. Journal of Food Science 53 231–236CrossRefGoogle Scholar
Mulvlhill, D. M., Rector, D. & Kinsella, J. E. 1990 Effects of structuring and destructuring anionic ions On the rheological properties of thermally-induced β-lactoglobulin gels. Food, Hydrocolloids 4 267–276Google Scholar
Myers-Betts, P. A. & Baianu, I. C. 1990 Approaches to protein hydration and water activity in food proteins by nuclear magnetic relaxation and vapor pressure equilibration techniques. Journal of Agricultural and food Chemistry 38 1171–1177CrossRefGoogle Scholar
Oakes, J. 1976 a Protein hydration. Nuclear magnetic resonance relaxation studies of the state of water in native bovine serum albumin solutions. Journal of the Chemical Society, Faraday Transactions I 72, 216–227Google Scholar
Oakes, J. 1976 b Thermally denatured proteins. Nuclear magnetic resonance, binding isotherm and chemical modification studies of thermally denatured bovine serum albumin. Journal of the Chemical Society, Faraday Transactions I 72, 228–237Google Scholar
Padua, G. W., Richardson, S. J. & Steinberg, M. P. 1991 Water associated with whey protein invcstigated by pulsed NMR. Journal of Food Science 56 1557–1561CrossRefGoogle Scholar
Pumpernik, D., Fajt, B., Lapanje, S. & Ažman, A. 1975 NMR relaxation study of the thermal denaturation of lysozyme. Zeitschrift für Naturforschung 30C 294–295CrossRefGoogle Scholar
Reddy, I. M. & Kinsella, J. E. 1990 Interaction of βlactoglobulin with K-casein in micelles as assessed by chymosin hydrolysis: effect of temprrature, heating time, β-lactoglobulin concentration, and pH. Journal of Agricultural and Food Chemistry 38 50–58CrossRefGoogle Scholar
Rowland, S. J. 1938 The determination of the nitrogen distribution in milk. Journal of Dairy Research 9 4246CrossRefGoogle Scholar
Rydzy, M. & Skrzynski, W. 1980 Investigation of β-galactosidase thermal denaturation by nuclear magnetic relaxation method. Studia, Biophysica 78 119–126Google Scholar