Related Experiment Video
Updated: Sep 15, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
Published on: June 23, 2018
Peroxyl radical-mediated oxidative crosslinking of faba and pea proteins: Differential aggregation behavior and
Javiera Camus1, María Carolina Moreno1, Camilo López-Alarcón2
1Departamento de Ingeniería Química y Bioprocesos, Facultad de Ingeniería, Pontificia Universidad Católica de Chile, Macul, Chile.
Abstract:
Faba and pea proteins are increasingly used as alternative proteins in plant-based food systems; however, their comparative susceptibility to oxidation by peroxyl radicals (ROO•) remains poorly understood. This study aimed to compare the oxidative behavior of faba and pea proteins, individually and in mixtures, using ROO• generated by thermolysis of AAPH (2,2'-azobis(2-methylpropionamidine) dihydrochloride), to elucidate how protein profile influences the oxidative pattern. Oxidation induced similar levels of hydroperoxides and carbonyls, without major changes in secondary structure. However, faba proteins exhibited greater formation of high-molecular-mass aggregates than pea proteins. In faba proteins, crosslinked species were associated with formation of di-tyrosine and di-tryptophan mainly involving legumin-α, whereas oxidation in pea proteins was primarily linked to modification of the ∼47 kDa vicilin fraction. These findings demonstrate that faba and pea proteins differ markedly in their oxidation-induced crosslinking behavior, highlighting the role of protein profile in modulating oxidative structural changes in plant-based protein systems.
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Protein Organization
The primary structure of a protein is its amino acid sequence.

