Analysis of the preferential mechanisms of denaturation of whey protein variants as a function of temperature and pH for the development of an optical sensor

Heather Taterka*, Manuel Castillo

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

A pH- and temperature-dependent study was conducted using reconstituted low-heat skim milk at pH 6.3, 6.7 and 7.1 heated for 10 min at 80 and 90 °C to evaluate the relationship between bound and aggregate whey protein and optical light backscatter response. Significant correlations were found between casein micelle particle size and bound whey protein, and light backscatter correlations existed with both bound and aggregate whey protein, thus optical light backscatter may be useful to determine both whey protein attachment to the casein micelle and the formation of whey protein aggregates.

Original languageEnglish
Pages (from-to)226-235
Number of pages10
JournalInternational Journal of Dairy Technology
Volume71
Issue number1
DOIs
Publication statusPublished - 1 Feb 2018

Keywords

  • Casein
  • Dairy biochemistry
  • Milk processing
  • Milk proteins
  • Particle size
  • Whey

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