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Carbonylation of myofibrillar proteins through the maillard pathway: effect of reducing sugars and reaction temperature.
J Agric Food Chem. 2013 Mar 27; 61(12):3140-7.JA

Abstract

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.

Authors+Show Affiliations

Department of Animal Production and Food Science, Food Technology, University of Extremadura, 10003 Cáceres, Spain.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23438261

Citation

Villaverde, Adriana, and Mario Estévez. "Carbonylation of Myofibrillar Proteins Through the Maillard Pathway: Effect of Reducing Sugars and Reaction Temperature." Journal of Agricultural and Food Chemistry, vol. 61, no. 12, 2013, pp. 3140-7.
Villaverde A, Estévez M. Carbonylation of myofibrillar proteins through the maillard pathway: effect of reducing sugars and reaction temperature. J Agric Food Chem. 2013;61(12):3140-7.
Villaverde, A., & Estévez, M. (2013). Carbonylation of myofibrillar proteins through the maillard pathway: effect of reducing sugars and reaction temperature. Journal of Agricultural and Food Chemistry, 61(12), 3140-7. https://doi.org/10.1021/jf305451p
Villaverde A, Estévez M. Carbonylation of Myofibrillar Proteins Through the Maillard Pathway: Effect of Reducing Sugars and Reaction Temperature. J Agric Food Chem. 2013 Mar 27;61(12):3140-7. PubMed PMID: 23438261.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Carbonylation of myofibrillar proteins through the maillard pathway: effect of reducing sugars and reaction temperature. AU - Villaverde,Adriana, AU - Estévez,Mario, Y1 - 2013/03/12/ PY - 2013/2/27/entrez PY - 2013/2/27/pubmed PY - 2013/12/16/medline SP - 3140 EP - 7 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 61 IS - 12 N2 - 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. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/23438261/Carbonylation_of_myofibrillar_proteins_through_the_maillard_pathway:_effect_of_reducing_sugars_and_reaction_temperature_ L2 - https://doi.org/10.1021/jf305451p DB - PRIME DP - Unbound Medicine ER -