Abstract
Whey protein isolate (WPI) at an 11.0% concentration spontaneously formed a gel at 25 °C in 6 M urea. As the pH was increased from 7 to 10, gel formation, from a viscous sol to an elastic network, was accelerated. Addition of N-ethylmaleimide up to 6 mM inhibited gelation. The sulfhydryl (SH) content of WPI decreased during urea incubation, especially with increasing pH. Electrophoretic analyses revealed the progressive disappearance of α-lactalbumin, β-lactoglobulin, and serum albumin during the gelation process with concomitant formation of polymers of these proteins. The spontaneous formation of gels in 6 M urea resulted from protein-protein cross-linkages via oxidation of thiol groups and SH-disulfide interchange reactions.
Original language | English |
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Pages (from-to) | 1887-1891 |
Number of pages | 5 |
Journal | Journal of Agricultural and Food Chemistry |
Volume | 38 |
Issue number | 10 |
DOIs | |
State | Published - 1990 |
ASJC Scopus subject areas
- General Chemistry
- General Agricultural and Biological Sciences