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Regulation of milk protein solubility by a whey-derived proline-rich peptide product

Published online by Cambridge University Press:  23 April 2013

Sophie N. Selby-Pham ,
Kate Howell ,
Hema Jegasothy ,
Paul Sheean ,
Tanoj Singh ,
Cheryl Taylor  and
Louise E. Bennett
Sophie N. Selby-Pham
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia Department of Agriculture and Food Systems, Melbourne School of Land and Environment, University of Melbourne, Parkville, Victoria, 3051, Australia
Kate Howell
Affiliation:
Department of Agriculture and Food Systems, Melbourne School of Land and Environment, University of Melbourne, Parkville, Victoria, 3051, Australia
Hema Jegasothy
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Paul Sheean
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Tanoj Singh
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Cheryl Taylor
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Louise E. Bennett*
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
*
*For correspondence; e-mail: louise.bennett@csiro.au
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Abstract

The effects of a bovine whey peptide product enriched in proline (wPRP) on the solubility of milk proteins were tested under ambient conditions or following heat treatment at 75 and 100 °C, for 1 and 15 min, followed by post-incubation storage at either ambient temperature or 4 °C for up to 7 d. wPRP promoted solubilisation of milk proteins in a concentration-dependent manner without heat treatment and also after heat treatment at 75 and 100 °C, and the effect was enhanced after storage under either ambient or refrigerated storage conditions. Interactions of wPRP and milk proteins were monitored by particle size analysis and tryptic digestion and specifically linked with solubilisation of αS1 casein (αS1-Cn), which supported observed changes in milk protein solubility. The results suggested that wPRP preferably prevented or reversed physical versus covalent protein aggregation, with the relaxation of hydrophobic interactions at 4 °C providing an additive effect. This application of wPRP represents a novel approach to stabilisation of dairy proteins following thermal processing with industrial usefulness yet to be explored.

Keywords

Protein aggregationproline-rich peptidehydrophobic interaction
Type
Research Article
Information
Journal of Dairy Research , Volume 80 , Issue 3 , August 2013 , pp. 291 - 299
Copyright
Copyright © Proprietors of Journal of Dairy Research 2013 

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