Tea Polyphenols Affect Oxidative Modification and Solution Stability of Myofibrillar Protein from Grass Carp (Ctenopharyngodon idellus)

Li, Xuepeng; Liu, Cikun; Wang, Jinxiang; Li, Wenxie; Lin, Boyan; Zhu, Wenhui; Xu, Yongxia; Shi, Yi Wei; Mi, Hongbo; Lǐ, Jiànróng

doi:10.1007/s11483-020-09635-x

Cited by 46 publications

(34 citation statements)

References 48 publications

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“…(2016) reported that 6 and 30 μmol/g GA significantly improved the elasticity and hardness of MP f gels while 150 μmol/g impaired gelation due to excessive aggregation and insolubility of proteins promoted by the high concentration of GA. Similar dose‐dependence phenomena have been noted for chlorogenic acid and tea polyphenols (Cao & Xiong, 2015; Li et al., 2020). The effects of different concentrations (0.05, 0.25, and 1.25 mM) of RosA on the gelling behavior of MP f as well as the characteristics of covalent MP f –phenol adducts were evaluated by Tang et al.…”

Section: Effect Of Phytophenol Binding On Structure‐related Muscle Protein Functionalitysupporting

confidence: 75%

Myoprotein–phytophenol interaction: Implications for muscle food structure‐forming properties

Guo

Xiong

2021

Comp Rev Food Sci Food Safe

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Phenolic compounds are commonly incorporated into muscle foods to inhibit lipid oxidation and modify product flavor. Those that are present in or extracted from plant sources (seeds, leaves, and stems) known as “phytophenols” are of particular importance in the current meat industry due to natural origins, diversity, and safety record. Apart from these primary roles as antioxidants and flavorings, phytophenols are now recognized to be chemically reactive with a variety of food constituents, including proteins. In processed muscle foods, where the structure‐forming ability is critical to a product's texture‐related quality attributes and palatability, the functional properties of proteins, especially gelation and emulsification, play an essential role. A vast amount of recent studies has been devoted to protein–phenol interactions to investigate the impact on meat product texture and flavor. Considerable efforts have been made to elucidate the specific roles of phytophenol interaction with “myoproteins” (i.e., muscle‐derived proteins) probing the structure‐forming process in cooked meat products. The present review provides an insight into the actions of phytophenols in modifying and interacting with muscle proteins with an emphasis on the reaction mechanisms, detection methods, protein functionality, and implications for structural characteristics and textural properties of muscle foods.

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Section: Effect Of Phytophenol Binding On Structure‐related Muscle Protein Functionalitysupporting

confidence: 75%

Myoprotein–phytophenol interaction: Implications for muscle food structure‐forming properties

Guo

Xiong

2021

Comp Rev Food Sci Food Safe

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“…Treatments of MP with 6 and 30 μmol/g chlorogenic acid significantly increased the viscoelasticity of MP gels while 150 μmol/g impaired the gelation due to excessive aggregation and insolubility [ 150 ]. Similarly, gallic acid and tea polyphenols have been shown to exert a dose-dependent effect on increasing the elasticity and hardness of MP gels [ 156 , 157 ]. Jia et al [ 158 ] found that the elasticity of MP gels was increased by rutin in the concentrations range of 10–100 µmol/g.…”

Section: Antioxidant Strategies For Modulating Protein Oxidationmentioning

confidence: 99%

Animal and Plant Protein Oxidation: Chemical and Functional Property Significance

Xiong

Guo

2020

Foods

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Protein oxidation, a phenomenon that was not well recognized previously but now better understood, is a complex chemical process occurring ubiquitously in food systems and can be induced by processing treatments as well. While early research concentrated on muscle protein oxidation, later investigations included plant, milk, and egg proteins. The process of protein oxidation involves both radicals and nonradicals, and amino acid side chain groups are usually the site of initial oxidant attack which generates protein carbonyls, disulfide, dityrosine, and protein radicals. The ensuing alteration of protein conformational structures and formation of protein polymers and aggregates can result in significant changes in solubility and functionality, such as gelation, emulsification, foaming, and water-holding. Oxidant dose-dependent effects have been widely reported, i.e., mild-to-moderate oxidation may enhance the functionality while strong oxidation leads to insolubilization and functionality losses. Therefore, controlling the extent of protein oxidation in both animal and plant protein foods through oxidative and antioxidative strategies has been of wide interest in model system as well in in situ studies. This review presents a historical perspective of food protein oxidation research and provides an inclusive discussion of the impact of chemical and enzymatic oxidation on functional properties of meat, legume, cereal, dairy, and egg proteins based on the literature reports published in recent decades.

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“…These residues are extremely sensitive to changes in the microenvironment involving polarizability, amounts of charged groups, and a variety of specific interactions. At present, the differences in the fluorescence spectra of aromatic amino acids have served as a basis for determining the physicochemical factors that induce protein conformational rearrangements or the changes of protein functional properties under other treatments (Li et al., 2020).…”

Section: Resultsmentioning

confidence: 99%

Physicochemical properties, protein conformation, and aggregate morphology of heated myosin from Hypophthalmichthys molitrix and Nemipterus virgatus mixtures

Shi

Lǐ

et al. 2020

Food Frontiers

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Tea Polyphenols Affect Oxidative Modification and Solution Stability of Myofibrillar Protein from Grass Carp (Ctenopharyngodon idellus)

Cited by 46 publications

References 48 publications

Myoprotein–phytophenol interaction: Implications for muscle food structure‐forming properties

Myoprotein–phytophenol interaction: Implications for muscle food structure‐forming properties

Animal and Plant Protein Oxidation: Chemical and Functional Property Significance

Physicochemical properties, protein conformation, and aggregate morphology of heated myosin from Hypophthalmichthys molitrix and Nemipterus virgatus mixtures

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