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Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway.

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TLDR
In this paper, the potential impact of protein oxidation on the functional properties of myofibrillar proteins (MP) was investigated in vitro for 12 days at 37 °C in the presence of Cu2+, Fe3+, and Mb in combination with H2O2 and analyzed at sampling times for chemical changes induced by oxidative reactions and functional properties.
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 Cu2+, Fe3+, and Mb in combination with H2O2 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 Cu2+/systems, leads to a fast and severe loss of MP functionality, including impaired water-holding, foaming, and gelling capacities. The imp...

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Citations
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Protein Oxidation in Processed Meat: Mechanisms and Potential Implications on Human Health.

TL;DR: The current understanding of meat processing techniques and their possible effects on the status of protein oxidation and nutritional value, as well as their possible implications on human health are explored.
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Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals

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Understanding postmortem biochemical processes and post-harvest aging factors to develop novel smart-aging strategies.

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References
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Journal ArticleDOI

The oxidative environment and protein damage

TL;DR: The major fate of oxidised proteins is catabolism by proteosomal and lysosomal pathways, but some materials appear to be poorly degraded and accumulate within cells, and the accumulation of such damaged material may contribute to a range of human pathologies.
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Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences

TL;DR: The demonstration shows that oxidative modification of proteins "marks" them for degradation by most common proteases and especially by the cytosolic multicatalytic proteinase from mammalian cells, and contributes substantially to the intracellular pool of catalytically inactive and less active, thermolabile forms of enzymes.
Journal ArticleDOI

Protein carbonyls in meat systems: a review

TL;DR: A comprehensive review of protein carbonylation in protein processing can be found in this paper, where the authors present the current knowledge on the mechanisms and consequences of protein carbonation in proteins.
Journal ArticleDOI

Protein oxidation in muscle foods: A review

TL;DR: This paper is devoted to review the most relevant findings on the occurrence and consequences of Pox in muscle foods and the efficiency of different anti-oxidant strategies against the oxidation of muscle proteins.
Journal ArticleDOI

Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure.

TL;DR: Combinations of various chemical radical scavengers revealed that .OH is the primary species responsible for alteration of BSA secondary and tertiary structure and may hold important clues for the mechanism(s) by which oxygen radicals can increase proteolytic susceptibility.
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