Carbonylation of Myofibrillar Proteins through the Maillard Pathway: Effect of Reducing Sugars and Reaction Temperature

Carbonylation is recognized as one of the most remarkable chemical modifications in oxidized proteins and is generally ascribed to the direct attack of free radicals to basic amino acid residues. The purpose of this work was to investigate the formation of specific carbonyls, α-aminoadipic and γ-glu...

Full description

Saved in:
Bibliographic Details
Published in:Journal of agricultural and food chemistry 2013-03, Vol.61 (12), p.3140-3147
Main Authors: Villaverde, Adriana, Estévez, Mario
Format: Article
Language:English
Subjects:
2-Aminoadipic Acid - analogs & derivatives
2-Aminoadipic Acid - chemistry
Animals
Carbohydrates - pharmacology
Copper Sulfate - pharmacology
food quality
foods
free radicals
Glutamates - chemistry
glycation
human health
Maillard reaction
Maillard Reaction - drug effects
Meat
Muscle Proteins - chemistry
myofibrillar proteins
Myofibrils - chemistry
oxidation
Protein Carbonylation - drug effects
proteins
pyridoxamine
reducing sugars
Swine
Temperature
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Carbonylation is recognized as one of the most remarkable chemical modifications in oxidized proteins and is generally ascribed to the direct attack of free radicals to basic amino acid residues. The purpose of this work was to investigate the formation of specific carbonyls, α-aminoadipic and γ-glutamic semialdehydes (AAS and GGS, respectively), in myofibrillar proteins (MP) through a Maillard-type pathway in the presence of reducing sugars. The present study confirmed the concurrent formation of protein carbonyls and advanced glycation end-products (AGEs) during incubation (80 °C/48 h) of MP (4 mg/mL) in the presence of reducing sugars (0.5 M). Copper irons (10 μM) were found to promote the formation of protein carbonyls, and a specific inhibitor of the Maillard reaction (0.02 M pyridoxamine) blocked the carbonylation process which emphasize the occurrence of a Maillard-type pathway. The Maillard-mediated carbonylation occurred in a range of reducing sugars (0.02–0.5 M) and reaction temperatures (4–110 °C) compatible with food systems. Upcoming studies on this topic may contribute further to shed light on the complex interactions between protein oxidation and the Maillard reaction and the impact of the protein damage on food quality and human health.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf305451p