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Porcine β-lactoglobulin does not undergo thermally induced gelation

Published online by Cambridge University Press:  01 June 2009

Daniel P. Gallagher ,
M. Gerard Lynch  and
Daniel M. Mulvihill
Daniel P. Gallagher
Affiliation:
Department of Food Chemistry, National Food Biotechnology Centre, University College, Cork, Irish Republic
M. Gerard Lynch
Affiliation:
Department of Food Chemistry, National Food Biotechnology Centre, University College, Cork, Irish Republic
Daniel M. Mulvihill
Affiliation:
Department of Food Chemistry, National Food Biotechnology Centre, University College, Cork, Irish Republic
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Abstract

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Type
Short Communications
Information
Journal of Dairy Research , Volume 63 , Issue 3 , August 1996 , pp. 479 - 482
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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References

REFERENCES

Alexander, L. J. & Beattie, C. W. 1992 Sequence of porcine β-lactoglobulin cDNA. Animal Genetics 23 263–265Google Scholar
AOAC 1970 Official Methods of Analysis of the Association of Official Analytical Chemists, 11th edn, p. 248. Washington, DC: AOACGoogle Scholar
Bevekidge, T., Toma, S. J. & Nakai, S. 1974 Determination of SH– and SS– groups in some food proteins using Ellman's reagent. Journal of Food Science 39 49–51CrossRefGoogle Scholar
Dalgalarrondo, M., Dufour, E., Bertrand-Harb, C., Chobert, J. M. & Haertlé, T. 1992 Purification and characterization of two porcine β-lactoglobulin variants by NaCl salting-out and reversed phase HPLC. Lait 72 35–42CrossRefGoogle Scholar
Greaser, M. L., Yates, L. D., Krzywicki, K. & Roelke, D. L. 1983 Electrophoretic methods for the separation and identification of muscle proteins. Proceedings, 36th Reciprocal Meat Conference 38 87–91Google Scholar
Kessler, E. & Brew, K. 1970 The whey proteins of pig's milk: isolation and characterization of a β-lactoglobulin. Biochimica et Biophysica Ada 200 449–458CrossRefGoogle ScholarPubMed
Kuwajima, K. 1989 The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Structure, Function and Genetics 6 87–103Google Scholar
Lee, S. P., Cho, Y. J. & Batt, C. A. 1993 Enhancing the gelation of β-lactoglobulin. Journal of Agricultural and Food Chemistry 41 1343–1348Google Scholar
McSwiney, M., Singh, H., Campanella, O. & Creamer, L. K. 1994 Thermal gelation and denaturation of bovine β-lactoglobulins A and B. Journal of Dairy Research 61 221–232Google Scholar
Matsudomi, N., Rector, D. & Kinsella, J. E. 1991 Gelation of bovine serum albumin and β-lactoglobulin; effects of pH, salts and thiol reagents. Food Chemistry 40 55–69Google Scholar
Morris, E. R. & Ross-Murphy, S. B. 1981 Chain flexibility of polysaccharides and glycoproteins from viscosity measurements. Techniques in the Life Sciences B308–3101–46Google Scholar
Mulvihill, D. M. & Kinsella, J. E. 1987 Gelation characteristics of whey proteins and β-lactoglobulin. Foal Technology 41 (9) 102, 104, 100, 108, 110–111Google Scholar
Mulvihill, D. M., Rector, D. & Kinsella, J. E. 1991 Mercaptoethanol, N-ethylmalcimide, propylene glycol and urea effects on rheological properties of thermally induced β-lactoglobulin gels at alkaline pH. Journal of Food Science 56 1338–1341CrossRefGoogle Scholar
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. 1986 The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324 383–385Google Scholar
Shimada, K. & Matsushita, S. 1980 Relationship between thermocoagulation of proteins and amino acid compositions. Journal of Agricultural and Food Chemistry 28 413–417CrossRefGoogle Scholar
Stading, M. & Hermansson, A. M. 1990 Viscoelastic behaviour of β-lactoglobulin gel structures. Food Hydrocolloids 4 121–135Google Scholar