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Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway.
J Agric Food Chem. 2012 Aug 15; 60(32):8002-11.JA

Abstract

The potential impact of protein oxidation on the functional properties of myofibrillar proteins (MP) was investigated in the present study. To accomplish this purpose, myofibrillar proteins were oxidized in vitro for 12 days at 37 °C in the presence of Cu(2+), Fe(3+), and Mb in combination with H(2)O(2) and analyzed at sampling times for chemical changes induced by oxidative reactions and functional properties. The oxidation measurements included specific protein carbonyls (α-aminoadipic semialdehyde, AAS), advanced lysine oxidation products (α-aminoadipic acid, AAA, and Schiff bases), and thiobarbituric acid-reactive substances (TBARS). The factors and mechanisms involved in the oxidative degradation of lysine residues through the carbonylation pathway are precisely described. According to the present results, intense lipid and protein carbonylation, principally induced by Cu(2+)/systems, leads to a fast and severe loss of MP functionality, including impaired water-holding, foaming, and gelling capacities. The implication of Mb in the oxidation events enhances the production of AAA and Schiff bases, compromising to a larger extent the solubility of MP and worsening the aggregation and the gelling capacity. The connection between the oxidation-induced chemical changes and the loss of protein functionality is thoroughly discussed.

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

22838408

Citation

Utrera, Mariana, and Mario Estévez. "Oxidation of Myofibrillar Proteins and Impaired Functionality: Underlying Mechanisms of the Carbonylation Pathway." Journal of Agricultural and Food Chemistry, vol. 60, no. 32, 2012, pp. 8002-11.
Utrera M, Estévez M. Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway. J Agric Food Chem. 2012;60(32):8002-11.
Utrera, M., & Estévez, M. (2012). Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway. Journal of Agricultural and Food Chemistry, 60(32), 8002-11. https://doi.org/10.1021/jf302111j
Utrera M, Estévez M. Oxidation of Myofibrillar Proteins and Impaired Functionality: Underlying Mechanisms of the Carbonylation Pathway. J Agric Food Chem. 2012 Aug 15;60(32):8002-11. PubMed PMID: 22838408.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway. AU - Utrera,Mariana, AU - Estévez,Mario, Y1 - 2012/08/06/ PY - 2012/7/31/entrez PY - 2012/7/31/pubmed PY - 2012/12/18/medline SP - 8002 EP - 11 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 60 IS - 32 N2 - The potential impact of protein oxidation on the functional properties of myofibrillar proteins (MP) was investigated in the present study. To accomplish this purpose, myofibrillar proteins were oxidized in vitro for 12 days at 37 °C in the presence of Cu(2+), Fe(3+), and Mb in combination with H(2)O(2) and analyzed at sampling times for chemical changes induced by oxidative reactions and functional properties. The oxidation measurements included specific protein carbonyls (α-aminoadipic semialdehyde, AAS), advanced lysine oxidation products (α-aminoadipic acid, AAA, and Schiff bases), and thiobarbituric acid-reactive substances (TBARS). The factors and mechanisms involved in the oxidative degradation of lysine residues through the carbonylation pathway are precisely described. According to the present results, intense lipid and protein carbonylation, principally induced by Cu(2+)/systems, leads to a fast and severe loss of MP functionality, including impaired water-holding, foaming, and gelling capacities. The implication of Mb in the oxidation events enhances the production of AAA and Schiff bases, compromising to a larger extent the solubility of MP and worsening the aggregation and the gelling capacity. The connection between the oxidation-induced chemical changes and the loss of protein functionality is thoroughly discussed. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/22838408/Oxidation_of_myofibrillar_proteins_and_impaired_functionality:_underlying_mechanisms_of_the_carbonylation_pathway_ L2 - https://doi.org/10.1021/jf302111j DB - PRIME DP - Unbound Medicine ER -