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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
Author(s) -
Taterka Heather,
Castillo Manuel
Publication year - 2018
Publication title -
international journal of dairy technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.061
H-Index - 53
eISSN - 1471-0307
pISSN - 1364-727X
DOI - 10.1111/1471-0307.12348
Subject(s) - whey protein , chemistry , micelle , casein , denaturation (fissile materials) , food science , skimmed milk , particle size , whey protein isolate , chromatography , nuclear chemistry , aqueous solution
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.