Protein carbonyls in meat systems: a review

https://cyberleninka.org/article/n/1240714.pdf

Designs, formats and applications of lateral flow assay: A literature review

Processed meats represent a large percentage of muscle foods consumed in the western world Various processing steps affect the physicochemical properties of the meat, compromise its nutritional components, or produce some compounds that are of health concern Hence, the impact of oxidation on human health and the aging process and the influence of diet on these harmful reactions are of growing interest Past decades have seen more focus on lipid oxidation, microbial deterioration, and pathogenicity, as well as production of carcinogenic compounds during meat processing The oxidation of protein, which is a major component in meat systems, has received less attention Protein oxidation has been defined as a covalent modification of protein induced either directly by reactive species or indirectly by reaction with secondary by-products of oxidative stress Not only are these modifications critical for technological and sensory properties of muscle foods, they may have implications on human health and safety when consumed Cooking, for example, has been observed to increase free radical generation while it also decreases the antioxidant protection systems in meat, both of which contribute to protein oxidation Many other meat processing techniques, as well as other emerging technologies, may significantly affect protein oxidation and protein overall quality This paper explores 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

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

Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein.

Berries extracts as natural antioxidants in meat products: A review.

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...

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

Protein oxidation during frozen storage and subsequent processing of different beef muscles.

This study examined the relationship between protein and lipid oxidation and the impairment of water holding capacity (WHC), colour and texture after frozen storage (20 weeks/−18 °C) and subsequent processing (cooking, chilled storage) of beef patties with increasing fat content (3, 20 and 35%). Various manifestations of protein oxidation were found to occur during frozen storage and processing of patties including, loss of tryptophan fluorescence, carbonylation and formation of Schiff bases structures (SB). Patties with higher fat content underwent the more intense protein oxidation as assessed by formation of protein carbonyls and SB, highlighting the timely interaction between proteins and oxidizing lipids. Protein oxidation occurred concomitantly with loss of WHC and discolouration of beef patties. Mechanisms and consequences of the chemical modifications induced by oxidative stress in meat proteins are thoroughly discussed.

Fat content has a significant impact on protein oxidation occurred during frozen storage of beef patties

The effects of the addition of avocado oil and a phenolic-rich avocado peel extract on protein oxidation were studied in porcine patties subjected to cooking and chilled storage. Protein oxidation was assessed by means of tryptophan loss and the formation of specific lysine oxidation products, such as α-aminoadipic semialdehyde (AAS), α-aminoadipic acid (AAA), and Schiff bases. In the present paper, quantitative data of AAA are reported for the first time on a food matrix. The addition of the avocado extract inhibited the formation of AAS, AAA, and Schiff bases in patties during cooking and subsequent chilled storage. The antioxidant effect may respond to the protecting effect of phenolic compounds, mainly procyanidins, found on the avocado extract. Apparently, the combination of both strategies (back-fat replacement and addition of avocado extract) does not lead to an enhanced advantage on the oxidative stability of the product. The novel methodologies used in the present study enable a better comprehension of the mechanisms and consequences of protein oxidation in food systems.

Mariana Utrera

Papers

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

Protein oxidation during frozen storage and subsequent processing of different beef muscles.

Fat content has a significant impact on protein oxidation occurred during frozen storage of beef patties

Formation of Lysine-Derived Oxidation Products and Loss of Tryptophan during Processing of Porcine Patties with Added Avocado Byproducts.

Temperature of frozen storage affects the nature and consequences of protein oxidation in beef patties