Protein-peptide interactions in mixtures of whey peptides and whey proteins
| Autor: | Harry Gruppen, Nathalie Creusot |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Whey protein
medicine.medical_treatment Bacillus Peptide Mass Spectrometry Hydrolysate Whey protein isolate Hydrophobic effect bovine beta-lactoglobulin Levensmiddelenchemie alpha-lactalbumin medicine Bacillus licheniformis Chromatography High Pressure Liquid VLAG chemistry.chemical_classification Protease Chromatography glu Food Chemistry biology Chemistry General Chemistry Milk Proteins biology.organism_classification Whey Proteins Biochemistry hydrolysis Ionic strength fractions biology.protein identification induced aggregation Peptides General Agricultural and Biological Sciences Peptide Hydrolases |
| Zdroj: | Journal of Agricultural and Food Chemistry 55 (2007) 6 Journal of Agricultural and Food Chemistry, 55(6), 2474-2481 |
| ISSN: | 0021-8561 2474-2481 |
| Popis: | The effects of several conditions on the amounts and compositions of aggregates formed in mixtures of whey protein hydrolysate, made with Bacillus licheniformis protease, and whey protein isolate were investigated using response surface methodology. Next, the peptides present in the aggregates were separated from the intact protein and identified with liquid chromatography-mass spectrometry. Increasing both temperature and ionic strength increased the amounts of both intact protein and peptides in the aggregates. There was an optimal amount of added intact WPI that could aggregate with peptides, yielding a maximal amount of aggregated material in which the peptide/protein molar ratio was around 6. Under all conditions applied, the same peptides were observed in the protein-peptide aggregates formed. The dominant peptides were beta-lg AB [f1-45], beta-lg AB [f90-108], and alpha-la [f50-113]. It was hypothesized that peptides could form a kind of glue network that can include beta-lactoglobulin via hydrophobic interactions at the hydrophobic binding sites at the surface of the protein. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|