Journal of Dairy Science
Volume 91, Issue 7 , Pages 2553-2560, July 2008

Factors Regulating Astringency of Whey Protein Beverages

  • J.W. Beecher

      Affiliations

    • Campbell Soup Company, Camden, NJ 08103
  • ,
  • M.A. Drake

      Affiliations

    • Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Raleigh 27695
  • ,
  • P.J. Luck

      Affiliations

    • Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Raleigh 27695
  • ,
  • E.A. Foegeding

      Affiliations

    • Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Raleigh 27695
    • Corresponding Author InformationCorresponding author.

Received 6 February 2008; accepted 12 March 2008.

Abstract 

A rapidly growing area of whey protein use is in beverages. There are 2 types of whey protein-containing beverages: those at neutral pH and those at low pH. Astringency is very pronounced at low pH. Astringency is thought to be caused by compounds in foods that bind with and precipitate salivary proteins; however, the mechanism of astringency of whey proteins is not understood. The effect of viscosity and pH on the astringency of a model beverage containing whey protein isolate was investigated. Trained sensory panelists (n = 8) evaluated the viscosity and pH effects on astringency and basic tastes of whey protein beverages containing 6%wt/vol protein. Unlike what has been shown for alum and polyphenols, increasing viscosity (1.6 to 7.7 mPa·s) did not decrease the perception of astringency. In contrast, the pH of the whey protein solution had a major effect on astringency. A pH 6.8 whey protein beverage had a maximum astringency intensity of 1.2 (15-point scale), whereas that of a pH 3.4 beverage was 8.8 (15-point scale). Astringency decreased between pH 3.4 and 2.6, coinciding with an increase in sourness. Decreases in astringency corresponded to decreases in protein aggregation as observed by turbidity. We propose that astringency is related to interactions between positively charged whey proteins and negatively charged saliva proteins. As the pH decreased between 3.4 and 2.6, the negative charge on the saliva proteins decreased, causing the interactions with whey proteins to decrease.

Key words: astringency, saliva, whey protein

 

PII: S0022-0302(08)71128-7

doi:10.3168/jds.2008-1083

Journal of Dairy Science
Volume 91, Issue 7 , Pages 2553-2560, July 2008