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- W3020841446 endingPage "242" @default.
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- W3020841446 abstract "The chemical and physical stability of the more common proteins of bovine and, where available, ovine, caprine, and equine whey (β-lactoglobulin, α-lactalbumin, serum albumin, immunoglobulins, and lactoferrin) is reviewed with regard to their molecular structures and dynamics. The behavior of the proteins separately and in combination with temperature, pressure, pH, denaturants (such as guanidinium chloride and urea), and stabilizers (such as fatty acids and metal ions) has been considered. The combination of high temperature and low pH in the hydrolysis and subsequent formation of fibrils constitutes a new body of study and knowledge since the first edition of this chapter in 2009. Particular emphasis has been placed on studies that have utilized x-ray, NMR, fluorescence, and circular dichroism techniques. Attention is directed to the role of cysteines and disulfide bridges with regard to chemical stability. Whereas there is considerable knowledge of structure–function relationships of individual proteins, there is a dearth of three-dimensional structural knowledge of combinations of proteins, despite the clear importance of such knowledge to functionality, especially with regard to food processes." @default.
- W3020841446 created "2020-05-13" @default.
- W3020841446 creator A5028603943 @default.
- W3020841446 creator A5073197925 @default.
- W3020841446 date "2014-01-01" @default.
- W3020841446 modified "2023-10-16" @default.
- W3020841446 title "Structure and Stability of Whey Proteins" @default.
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