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Gelling properties of microparticulated whey proteins

Dissanayake, Muditha, Kelly, Alan L and Vasiljevic, Todor (2010) Gelling properties of microparticulated whey proteins. Journal of Agricultural and Food Chemistry, 58 (11). pp. 6825-6832. ISSN 0021-8561

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Abstract

Subjecting whey proteins to high-pressure shearing with or without heating, commonly termed microparticulation, results in novel ingredients with modulated functionalities. Gelling properties of microparticulated whey proteins (MWP) were specifically assessed in this study. MWP powders were produced from commercial cheese whey retentate, standardized to 10% (w/w) protein, and subjected to microfluidization (MFZ) at 140 MPa either with or without prior heat-induced denaturation, followed by spray-drying. Gels were created from aqueous MWP dispersions either by heating at 90 �C for 20 min or by allowing gels to form at ambient temperature through addition of glucano-δ- lactone and/or NaCl. MWP powders produced from unheated WP dispersions created firm gels upon heating, whereas those produced from denatured WP gave only cold-set gels. Covalent and noncovalent protein-protein interactions were involved during both heat- and cold-induced gelation. Hydrophobic interactions were more pronounced during aggregation of bovine serum albumin. In conclusion, microparticulation of WP resulted in heat- and cold-set gels with different molecular and physical characteristics from those of untreated controls.

Item Type: Article
Uncontrolled Keywords: ResPubID19805, whey proteins, microfluidization, cold gelation, heat gelation, polyacrylamide gel electrophoresis, N-ethylmaleimide, sodium dodecyl sulfate, Tween 20
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 0908 Food Sciences
SEO Classification > 8602 Dairy Products
Depositing User: VUIR
Date Deposited: 20 Dec 2011 00:50
Last Modified: 10 Mar 2015 04:13
URI: http://vuir.vu.edu.au/id/eprint/7360
DOI: https://doi.org/10.1021/jf1009796
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Citations in Scopus: 34 - View on Scopus

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