Whey proteins are commonly used as ingredient in food. In relation with the gelation properties of whey proteins, this thesis deals with understanding the mechanism of peptide-induced aggregation of whey protein hydrolysates made with Bacillus licheniformis protease (BLP). The results show that BLP breaks down hydrophilic segments in the substrate and, therefore, preserves hydrophobic segments that aggregate once exposed to the solvent. Aggregation during hydrolysis prevented further degradation of the substrate, explaining that aggregating peptides are larger than the non-aggregating ones. Solubility experiments performed on fractionated aggregating peptides showed that peptide co-aggregation is an important factor in the aggregation process. Results also showed that the hydrolysates are able to aggregate added parental protein. The aggregating peptides could form a network in which the presence of both insoluble and partly insoluble peptides was required for the aggregation of intact protein.
|Qualification||Doctor of Philosophy|
|Award date||13 Nov 2006|
|Place of Publication||[S.l.]|
|Publication status||Published - 2006|
- whey protein
- bacillus licheniformis