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Heat-related changes to the hydrophobicity of cheese whey correlate with levels of native β-lactoglobulin and α-lactalbumin

Published online by Cambridge University Press:  01 June 2009

Geoffrey O. Regester ,
R. John Pearce ,
Victor W. K. Lee  and
Michael E. Mangino
Geoffrey O. Regester
Affiliation:
Dairy Research Laboratory, CSIRO Division of Food Processing, Highett, Victoria 3190, Australia
R. John Pearce
Affiliation:
Dairy Research Laboratory, CSIRO Division of Food Processing, Highett, Victoria 3190, Australia
Victor W. K. Lee
Affiliation:
Department of Biological Sciences, Deakin University, Geelong, Victoria 3217, Australia
Michael E. Mangino
Affiliation:
Department of Food Science and Technology, The Ohio State University, Columbus, OH 43210, USA
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Summary

Correlations were identified between levels of the native whey proteins, β-lactoglobulin and α-lactalbumin and the surface and total hydrophobicities of cheese whey in response to different heat treatments. Heat-induced changes in the native βlactoglobulin content and surface hydrophobicity of whey exhibited the most significant linear relationship while correlations between total hydrophobicity and the native proteins were less significant because of an atypical rise in the n−heptane-binding capacity of whey after high-temperature treatment. The content of native β-lactoglobulin in whey was more sensitive to heating than the content of native α-lactalbumin, while heat-related changes in the total hydrophobicity of whey were generally greater than similar changes in surface hydrophobicity.

Type
Original Articles
Information
Journal of Dairy Research , Volume 59 , Issue 4 , November 1992 , pp. 527 - 532
Copyright
Copyright © Proprietors of Journal of Dairy Research 1992

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References

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