Journal
FOOD CHEMISTRY
Volume 289, Issue -, Pages 223-231Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2019.02.114
Keywords
Beta-Lactoglobulin; Amyloid aggregates; Fibrils; Protein oxidation
Funding
- German Research Foundation (DFG) [SPP 1934 DiSPBiotech, 273937032]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available