MALDI based identification of whey protein derived tryptic marker peptides that resist protein glycation
Autor: | Barbara Kerkaert, Bart Devreese, Bruno De Meulenaer, Tatiana Cucu, Isabel Vandenberghe |
---|---|
Rok vydání: | 2012 |
Předmět: |
chemistry.chemical_classification
Whey protein biology Chemistry Lysine food and beverages medicine.disease Tandem mass spectrometry Polysaccharide Maillard reaction symbols.namesake Biochemistry Food allergy medicine biology.protein symbols Food science Protein glycation Beta-lactoglobulin Food Science |
Zdroj: | Food Research International. 47:23-30 |
ISSN: | 0963-9969 |
Popis: | Cow's milk and dairy products are a common cause of food allergy especially for children. The extensive use of milk proteins, especially whey, in food products poses a serious threat to allergic consumers, therefore reliable detection methods are needed in order to ensure meticulous labeling and to protect allergic consumers. The aim of the study was to do a screening of the tryptic peptides derived from whey proteins which were still identifiable using MALDI-TOF/MS and MS/MS analysis despite severe modification through food processing simulating reactions. A bottom-up approach was therefore used. Whey protein mixtures were subjected to the Maillard reaction with glucose, both in the absence or presence of soluble wheat proteins. Despite severe changes on protein level as evidenced by a time dependent increase of protein bound carbonyls, fluorescent compounds, and aggregation as well as a parallel decrease of available lysine residues, several peptides were proven to remain stable. Using MALDI-TOF/MS and MS/MS analysis of tryptic digests of the glycated proteins, two unmodified peptides derived from β-lactoglobulin were identified ( 15 Val–Arg 40 and 41 Val–Lys 60 ). These stable peptides could serve as analytical targets for the development of new robust analytical approaches for detection of undeclared whey protein residues in foods. |
Databáze: | OpenAIRE |
Externí odkaz: |