Chemistry

Amyloid β

Amyloid beta

Amyloid (mycology)

Peptide

Biophysics

Amyloid fibril

Disease

Biology

Internal medicine

Inorganic chemistry

Whey protein

Beta-lactoglobulin

Tyrosine

Medicine

Protein aggregation

Fibril

Biochemistry

Food Chemistry

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.

Protein oxidation during temperature-induced amyloid aggregation of beta-lactoglobulin