4.7 Article

Gelling Properties of Microparticulated Whey Proteins

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 58, Issue 11, Pages 6825-6832

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf1009796

Keywords

Whey proteins; microfluidization; cold gelation; heat gelation; polyacrylamide gel electrophoresis; N-ethylmaleimide; sodium dodecyl sulfate; Tween 20

Funding

  1. Faculty of Health, Engineering and Science, Victoria University, Melbourne
  2. Dairy Innovation of Australia Limited

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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 degrees C for 20 min or by allowing gels to form at ambient temperature through addition of glucano-delta-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.

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