Protein oxidation during temperature-induced amyloid aggregation of beta-lactoglobulin.
Food Chem
; 289: 223-231, 2019 Aug 15.
Article
em En
| MEDLINE
| ID: mdl-30955606
ABSTRACT
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 72â¯h. After 5â¯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 72â¯h, the building blocks at both pH values changed towards smaller peptides. The apparent tyrosine oxidation reached a maximum after 5â¯h at both pH values, whereas N-formylkynurenine and carbonyls increased continuously during 72â¯h. In case amyloid structures are used as edible material, the health related effects caused by protein oxidation needs to be considered.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Agregados Proteicos
/
Lactoglobulinas
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article