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:
Affiliation:
1. Departament de Ciència Animal i dels Aliments; Universitat Autònoma de Barcelona; Campus de la UAB 08193 Bellaterra, Cerdanyola del Vallés, Barcelona Spain
Funder
Marie Curie FP7-Reintegration-Grant, 2010
Publisher
Wiley
Subject
Process Chemistry and Technology,Bioengineering,Food Science
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/1471-0307.12348/fullpdf
Reference39 articles.
1. Role of kappa-casein in the association of denatured whey proteins with casein micelles in heated reconstituted skim milk;Anema;Journal of Agricultural and Food Chemistry,2007
2. On heating milk, the dissociation of kappa-casein from the casein micelles can precede interactions with the denatured whey proteins;Anema;The Journal of Dairy Research,2008a
3. The whey proteins in milk: thermal denaturation, physical interactions and effects on the functional properties of milk
4. Further studies on the heat-induced, pH-dependent dissociation of casein from the micelles in reconstituted skim milk;Anema;LWT - Food Science and Technology,2000
5. Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size;Anema;The Journal of Dairy Research,2003a
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2. Thermal Denaturation of Milk Whey Proteins: A Comprehensive Review on Rapid Quantification Methods Being Studied, Developed and Implemented;Dairy;2022-07-18
3. Effect of pH on heat-induced interactions in high-protein milk dispersions and application of fluorescence spectroscopy in characterizing these changes;Journal of Dairy Science;2021-04
4. The effect of heat treatment on the front-face fluorescence spectrum of tryptophan in skim milk;Journal of Food Composition and Analysis;2020-09
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