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Protein oxidation during temperature-induced amyloid aggregation of beta-lactoglobulin
- Keppler, Julia K., Heyn, Timon R., Meissner, Philipp M., Schrader, Katrin, Schwarz, Karin
- Food chemistry 2019 v.289 pp. 223-231
- amyloid, beta-lactoglobulin, oxidation, pH, peptides, tyrosine
- Although the connection between protein oxidation, amyloid aggregation and diseases such as Alzheimer’s is well known there is no information on such effects during preparation of beta-lactoglobulin fibrils. Different morphologies of amyloid aggregates of beta-lactoglobulin were prepared by incubation at pH 2 or pH 3.5 for up to 72 h. After 5 h, amyloid aggregates at pH 2 formed typical fibrils, which consisted of peptides. At pH 3.5, the amyloid aggregates were worm-like and consisted of intact protein. After 72 h, the building blocks at both pH values changed towards smaller peptides. The apparent tyrosine oxidation reached a maximum after 5 h at both pH values, whereas N-formylkynurenine and carbonyls increased continuously during 72 h. In case amyloid structures are used as edible material, the health related effects caused by protein oxidation needs to be considered.