Modulation of amyloid fibrillation of bovine β-lactoglobulin by selective methionine oxidation.

ABSTRACT: Deposition of oxidation-modified proteins during normal aging and oxidative stress are directly associated with systemic amyloidoses. Methionine (Met) is believed to be one of the most readily oxidisable amino acid residues of protein. Bovine beta-lactoglobulin (β-lg), a model globular whey protein, has been presented as a subsequent paradigm for studies on protein aggregation and amyloid formation. Herein, we investigated the effect of t-butyl hydroperoxide (tBHP)-induced oxidation on structure, compactness and fibrillation propensity of β-lg at physiological pH. Notably, whey protein modification, specifically Met residues, plays an important role in the dairy industry during milk processing and lowering nutritional value and ultimately affecting their technological propert

SUBMITTER: Maity S 

PROVIDER: S-EPMC8695858 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature