Apple phenolics as inhibitors of the carbonylation pathway during in vitro metal-catalyzed oxidation of myofibrillar proteins

Rysman, Tine; Utrera, Mariana; Morcuende, David; Royen, Geert Van; Weyenberg, Stéphanie Van; Smet, Stefaan De; Estévez, Mario

doi:10.1016/j.foodchem.2016.05.126

Cited by 35 publications

(11 citation statements)

References 39 publications

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“…The progress in the understanding of the biological significance of protein oxidation has been enabled by the elucidation of the molecular basis of the initiation, progression, and formation of protein oxidation products. Often criticized for the restricted application of their results to complex food systems, mechanistic studies in model systems have been highly valuable to provide insight into the chemistry of protein oxidation (Bao, Boeren, & Ertbjerg, ; Chen, Diao, Li, Chen, & Kong, ; Geng et al., ; Jongberg et al., ; Luna, & Estévez, ; Rysman et al., ; Yang & Xiong, ). The oxidation of proteins has been recognized as a complex chain reaction owing to the variety of mechanisms and oxidation products potentially formed (Dean et al., ).…”

Section: Chemistry Fundamentals: a Concise Updatementioning

confidence: 99%

Intake of Oxidized Proteins and Amino Acids and Causative Oxidative Stress and Disease: Recent Scientific Evidences and Hypotheses

Estévez

Xiong

2019

Journal of Food Science

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113

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The exposure to reactive oxygen species (ROS) is an inevitable consequence of living in an aerobic world. The species contribute to the occurrence of oxidative stress in humans in which an uncontrolled production of ROS exceeds the endogenous antioxidant defences leading to the oxidative damage to essential cellular components, such as lipids, proteins, and DNA. The influence of diet on the modulation of the systemic redox status is recognized and, while some dietary components are found to be protective (that is, fruits and vegetables), others are recognized as pro‐oxidants (that is, processed meat and other animal‐source protein foods). Oxidized proteins and amino acids are potential promoters of luminal and postprandial oxidative stress; preliminary studies have actually reported noxious effects of these species in cultured cells and in experimental animals. However, the underlying pathological mechanisms remain poorly understood. The application of advanced methodological approaches based on mass spectrometric technologies and OMICS disciplines has enabled the elucidation of the molecular basis of the pathological effects of dietary oxidized proteins and amino acids. The present review collects the most recent evidences of the health risks of dietary protein oxidation and proposes reasonable hypotheses and future perspectives on the field.

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Section: Chemistry Fundamentals: a Concise Updatementioning

confidence: 99%

Intake of Oxidized Proteins and Amino Acids and Causative Oxidative Stress and Disease: Recent Scientific Evidences and Hypotheses

Estévez

Xiong

2019

Journal of Food Science

Self Cite

113

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“…Oxidation of protein and protein carbonylation are often associated with altered protein functionality, resulting in deteriorated texture, flavor, water holding capacity, and nutritional quality (Lund et al 2011). With regards to protein carbonylation, a recent study indicated that apple peel phenolics chlorogenic acid, (-)epicatechin and phloridzin inhibited the formation of specific protein carbonyl products in oxidized pork myofibrillar proteins, suggesting their role as natural inhibitor of protein carbonylation (Rysman et al 2016). Additionally, quercetin, a flavonol from apple peel, showed potent antioxidant activity against protein oxidation, mainly due to its radical scavenging activity derived from the 3 0 ,4 0 -dihydroxy group located on the B ring (Utrera and Estévez 2013).…”

Section: Protein Oxidationmentioning

confidence: 99%

Effect of apple peel extract as natural antioxidant on lipid and protein oxidation of rainbow trout (Oncorhynchus mykiss) mince

et al. 2019

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The aim of this study was to use apple peel extract (APE) as antioxidant for inhibition of lipid and protein oxidation in rainbow trout (Oncorhynchus mykiss) mince during refrigerated storage. Apple peel extract had high 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2 0-azinobios-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and hydroxyl radical scavenging activity and ferric reducing antioxidant power (FRAP) comparable to ascorbic acid. Lipid oxidation was effectively inhibited in mince during 96 h of refrigerated storage as indicated by significantly lower peroxides and thiobarbituric acid-reactive substances (TBARS) (P \ 0.05) compared to control. APE could reduce protein oxidation as evidenced by lower protein carbonyls and higher total sulfhydryl group content (P \ 0.05) compared to control. This was coincidental with higher polyunsaturated fatty acids (PUFA)/saturated fatty acids (SFA) and eicosapentaenoic acid (EPA) ? docosahexaenoic acid (DHA)/palmitic acid (C16:0) ratio in mince with added apple peel extract, especially at 20 mg of gallic acid equivalent/kg mince. Apple peel extract retarded fish mince lipid and protein oxidation during refrigerated storage and might be considered as natural antioxidant in rainbow trout mince.

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“…The findings in our study are in good agreement with a previous report from Rysman et al which concluded that phenolic compounds in apple (chlorogenic acid, EC and phloridzin as well as an apple peel extract) were capable of curtailing protein oxidation in MP for 10 days. 27 However, conflicting results have been obtained in employing natural phenolic compounds in retarding protein oxidation. Certain redox-active phenolic compounds can be transformed into corresponding quinone derivatives which may accelerate protein carbonylation as pro-oxidant agents.…”

Section: Resultsmentioning

confidence: 99%

Influence of epicatechin on oxidation‐induced physicochemical and digestibility changes in porcine myofibrillar proteins during refrigerated storage

Sun

et al. 2020

J Sci Food Agric

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BACKGROUND: The influence of epicatechin (EC) on the physicochemical properties and digestibility changes of porcine myofibrillar protein (MP) under oxidative stress during refrigerated storage was investigated. RESULTS: The incubation of MP suspensions (20 mg mL −1 in piperazine-N,N 0-bis(2-ethanesulfonic acid) buffer, with 0.6 mol L −1 sodium chloride, pH 6.25) at 4°C for 24 h under an iron-catalyzed hydroxyl radical generating system (Fenton reaction) promoted the formation of thiobarbituric acid reactive substances and protein carbonyls, which was attenuated by EC (5, 50, and 100 ∼mol g −1 protein). Reduced protein sulfhydryl content, tryptophan fluorescence, protein solubility, as well as increased surface hydrophobicity were found by the co-incubation of EC. Analysis by scanning electron microscopy revealed increased protein aggregation and fragments in oxidized MP, which were further enhanced by the addition of EC. However, the protein digestibility of MP was not affected. CONCLUSION: EC was demonstrated to be effective in alleviating lipid oxidation and protein carbonylation in MP under oxidative stress. Additionally, the physicochemical and digestibility changes accompanying the incorporation of EC was complicated due to the possible phenol-protein interactions. An in-depth understanding of protein physicochemical and digestibility changes will be helpful in the application of polyphenolic compounds as antioxidants in low-temperature-processed muscle foods.

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Apple phenolics as inhibitors of the carbonylation pathway during in vitro metal-catalyzed oxidation of myofibrillar proteins

Cited by 35 publications

References 39 publications

Intake of Oxidized Proteins and Amino Acids and Causative Oxidative Stress and Disease: Recent Scientific Evidences and Hypotheses

Intake of Oxidized Proteins and Amino Acids and Causative Oxidative Stress and Disease: Recent Scientific Evidences and Hypotheses

Effect of apple peel extract as natural antioxidant on lipid and protein oxidation of rainbow trout (Oncorhynchus mykiss) mince

Influence of epicatechin on oxidation‐induced physicochemical and digestibility changes in porcine myofibrillar proteins during refrigerated storage

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