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      Protein Oxidation in Processed Meat: Mechanisms and Potential Implications on Human Health : Protein oxidation, nutrition, and health…

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      Comprehensive Reviews in Food Science and Food Safety
      Wiley-Blackwell

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          Protein carbonyls in meat systems: a review.

          Protein oxidation (P-OX) is an innovative topic of increasing interest among meat researchers. Carbonylation is generally recognized as one of the most remarkable chemical modifications in oxidized proteins. In fact, the quantification of protein carbonyls by the dinitrophenylhydrazine (DNPH) method is the most common procedure for assessing P-OX in meat systems. Numerous studies have investigated the occurrence of protein carbonylation right after slaughter and during subsequent processing and cold storage of meat. However, the significance of protein carbonylation in meat systems is still poorly understood. Beyond their role as markers of protein oxidation, specific protein carbonyls such as α-aminoadipic and γ-glutamic semialdehydes (AAS and GGS, respectively) are active compounds that may be implicated in several chemical reactions with relevant consequences on meat quality. The formation of protein carbonyls from particular amino acid side chains contribute to impair the conformation of myofibrillar proteins leading to denaturation and loss of functionality. Recent studies also highlight the potential impact of specific protein carbonyls in particular meat quality traits such as water-holding capacity (WHC), texture, flavor and its nutritional value. As a truly emerging topic, the results from current studies provide grounds from the development of further investigations. The present paper reviews the current knowledge on the mechanisms and consequences of protein carbonylation in meat systems and aims to encourage meat researchers to accomplish further investigations on this fascinating research topic.
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            2-Aminoadipic acid is a biomarker for diabetes risk.

            Improvements in metabolite-profiling techniques are providing increased breadth of coverage of the human metabolome and may highlight biomarkers and pathways in common diseases such as diabetes. Using a metabolomics platform that analyzes intermediary organic acids, purines, pyrimidines, and other compounds, we performed a nested case-control study of 188 individuals who developed diabetes and 188 propensity-matched controls from 2,422 normoglycemic participants followed for 12 years in the Framingham Heart Study. The metabolite 2-aminoadipic acid (2-AAA) was most strongly associated with the risk of developing diabetes. Individuals with 2-AAA concentrations in the top quartile had greater than a 4-fold risk of developing diabetes. Levels of 2-AAA were not well correlated with other metabolite biomarkers of diabetes, such as branched chain amino acids and aromatic amino acids, suggesting they report on a distinct pathophysiological pathway. In experimental studies, administration of 2-AAA lowered fasting plasma glucose levels in mice fed both standard chow and high-fat diets. Further, 2-AAA treatment enhanced insulin secretion from a pancreatic β cell line as well as murine and human islets. These data highlight a metabolite not previously associated with diabetes risk that is increased up to 12 years before the onset of overt disease. Our findings suggest that 2-AAA is a marker of diabetes risk and a potential modulator of glucose homeostasis in humans.
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              Protein oxidation: basic principles and implications for meat quality.

              The involvement of oxidized proteins to the development of biological diseases has been studied for a few decades, but the effects and the mechanisms of protein oxidation in food systems are largely unknown. Protein oxidation is defined as the covalent modification of a protein induced either by the direct reactions with reactive oxygen species (ROS) or indirect reactions with secondary by-products of oxidative stress. ROS can cause oxidation in both amino acid side chains and protein backbones, resulting in protein fragmentation or protein-protein cross-linkages. Although all amino acids can be modified by ROS, cysteine, and methionine that are the most susceptible to oxidative changes due to high reaction susceptibility of the sulfur group in those amino acids. Oxidative modifications of proteins can change their physical and chemical properties, including conformation, structure, solubility, susceptibility to proteolysis, and enzyme activities. These modifications can be involved in the regulation of fresh meat quality and influence the processing properties of meat products. Oxidative stress occurs when the formation of oxidants exceeds the ability of antioxidant systems to remove the ROS in organisms. Increased levels of protein oxidation have been associated with various biological consequences, including diseases and aging, in humans and other animal species. The basic principles and products of protein oxidation and the implications of protein oxidation in food systems, especially in meat, are discussed in this review.
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                Author and article information

                Journal
                Comprehensive Reviews in Food Science and Food Safety
                COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY
                Wiley-Blackwell
                15414337
                March 2015
                March 2015
                : 14
                : 2
                : 106-122
                Article
                10.1111/1541-4337.12127
                33401805
                ed3ca519-c9b1-40c7-aed8-f2e5a19bbaee
                © 2015

                http://doi.wiley.com/10.1002/tdm_license_1.1

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