Effect of hydroxyl-radical on the biochemical properties and structure of myofibrillar protein from Alaska pollock (Theragra chalcogramma)

Nyaisaba, Bhoke Marwa; Liu, Xinxin; Zhu, Shengli; Fan, Xiaodong; Sun, Linlin; Hatab, Shaimaa; Miao, Wenhua; Chen, Mei‐Ling; Deng, Shanggui

doi:10.1016/j.lwt.2019.02.045

Cited by 68 publications

(33 citation statements)

References 26 publications

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“…Under iron‐catalyzed oxidation, obvious fragmentation was observed, and the surface structure of MP exhibited more uneven shapes with some spread pores and protein aggregates. The change of surface structure under oxidative treatment was comparable to some previous studies, suggesting the presence of protein intramolecular and intermolecular crosslinking, aggregates and even degradation in proteins 39‐41 . In the presence of EC, fragmentation and agglomerate arrangement were promoted, and severe protein aggregation was observed when the concentration of EC reaches 100 μmol g −1 protein.…”

Section: Resultssupporting

confidence: 86%

“…The change of surface structure under oxidative treatment was comparable to some previous studies, suggesting the presence of protein intramolecular and intermolecular crosslinking, aggregates and even degradation in proteins. [39][40][41] In the presence of EC, fragmentation and agglomerate arrangement were promoted, and severe protein aggregation was observed when the concentration of EC reaches 100 μmol g −1 protein. The irregular microstructures caused by both oxidative stress and incorporation of EC suggested the complexity of protein-polyphenol interactions via covalent bindings which might be the result of lipid oxidation/ nucleophilic addition and non-covalent forces (hydrogen bonding, van der Waals forces, and hydrophobic bonding, etc.).…”

Section: Microstructurementioning

confidence: 99%

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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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Section: Resultssupporting

confidence: 86%

Section: Microstructurementioning

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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“…Lu et al [55] reported that treatment with H 2 O 2 increased protein surface hydrophobicity of bighead carp proteins. Nyaisaba et al [56] observed a similar result in MPs from Alaska pollock exposed to hydroxyl radicals. These findings are consistent with the results of the current study.…”

Section: Resultsmentioning

confidence: 65%

Ultrasonic structural modification of myofibrillar proteins from Coregonus peled improves emulsification properties

Deng

Lei

et al. 2021

Ultrasonics Sonochemistry

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“…Oxidation made the surface of the gel appear rough, with tiny pores. This may be attributed to changes in the forces between MP molecules caused by oxidation, and the speed of protein unfolding and aggregation affected the changes in microstructure (Nyaisaba et al, 2019 (Tang et al, 2017).…”

Section: Scanning Electron Microscope (Sem)mentioning

confidence: 99%

Effect of rutin on the physicochemical and gel characteristics of myofibrillar protein under oxidative stress

Guo

Hu²,

Wang

et al. 2021

J Food Biochem

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Oxidation is inevitable in meat storage, transportation, processing, and production. Reactive oxygen species (ROS) are the main substances that induce protein oxidation. The cell metabolism of the muscle itself produces a series of ROS free radicals, such as hydroxyl radicals (OH), peroxy radicals (ROO), and superoxide anions (O − 2 ).Among them, hydroxyl radicals are the most active free radicals (Gutteridge, 1994). Protein oxidation is a covalent modification that can either react directly with ROS or indirectly through secondary by-products of oxidative stress (Soladoye et al., 2015). It is the main reason for the loss of protein nutrients and digestive capacity, structural changes, and instability, as well as a decline in functional prop-

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Effect of hydroxyl-radical on the biochemical properties and structure of myofibrillar protein from Alaska pollock (Theragra chalcogramma)

Cited by 68 publications

References 26 publications

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

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

Ultrasonic structural modification of myofibrillar proteins from Coregonus peled improves emulsification properties

Effect of rutin on the physicochemical and gel characteristics of myofibrillar protein under oxidative stress

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