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A detailed investigation of whey protein isolate solutions and gels reveals a number of novel characteristics
CSIRO, Australia ; University of Melbourne, Australia.
RISE - Research Institutes of Sweden, Bioscience and Materials, Agrifood and Bioscience.
University of Melbourne, Australia.
2018 (English)In: Food Hydrocolloids, ISSN 0268-005X, E-ISSN 1873-7137, Vol. 77, p. 566-576Article in journal (Refereed) Published
Abstract [en]

The structure and rheology of whey proteins at a concentration of 10 % has been investigated as a function of pH. The turbidity of whey protein isolate (WPI) solutions was measured and DSC thermograms were run on samples at 0.2 pH unit intervals. The structure of heat-set gels prepared from these solutions was investigated by confocal laser scanning microscopy and gel strengths and fracture behaviour was also examined. From the DSC studies the maximum denaturation onset temperature of β-lg under these conditions was found to be 3.4 ± 0.2. A number of pH regions were identified where significant physical changes were found. Differences between the two transition regions between fine-stranded and spherical aggregates have been discussed and potential reason put forward. General trends were identified and an anomalous region at pH 6.2 (possibly related to the Tanford transition) was found in all of the properties of the solutions and gels investigated. This work provides a more detailed investigation into a range of structural and behavioural features of WPI gels over the acidic pH range than is currently available in the literature.

Place, publisher, year, edition, pages
2018. Vol. 77, p. 566-576
Keywords [en]
Whey protein isolate, pH, gel, fracture behaviour, microstructure, heat-set gelation
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-33156DOI: 10.1016/j.foodhyd.2017.10.035Scopus ID: 2-s2.0-85034451800OAI: oai:DiVA.org:ri-33156DiVA, id: diva2:1178026
Available from: 2018-01-26 Created: 2018-01-26 Last updated: 2018-05-04Bibliographically approved

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