Structural and gelation properties of five polyphenols-modified pork myofibrillar protein exposed to hydroxyl radicals

Cheng, Jingrong; Lin, Yaosheng; Tang, Daobang; Yang, Huaigu; Liu, Xueming

doi:10.1016/j.lwt.2022.113073

Cited by 17 publications

(11 citation statements)

References 37 publications

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“…To date, most studies on protein modification by polyphenols have focused on myofibrillar proteins. For example, various phenolic compounds have been shown to improve the gelation of porcine myofibrillar proteins [ 25 ]. Anqi Guo found that the formation of quinones by oxidizing gallic acid is conducive to the development of more elastic myofibrillar protein gels [ 26 ].…”

Section: Introductionmentioning

confidence: 99%

Alkali-Induced Phenolic Acid Oxidation Enhanced Gelation of Ginkgo Seed Protein

Zhang

Liu

Zhao

et al. 2023

Foods

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The effect of alkali-induced oxidation of three phenolic acids, namely gallic acid, epigallocatechin gallate, and tannic acid, on the structure and gelation of ginkgo seed protein isolate (GSPI) was investigated. A mixture of 12% (w/v) GSPI and different concentrations of alkali-treated phenolic acids (0, 0.06, 0.24, and 0.48% w/w) were heated at 90 °C, pH 6.0, for 30 min to form composite gels. The phenolic treatment decreased the hydrophobicity of the GSPI sol while enhancing their rheological properties. Despite a reduced protein solubility, water holding capacity, stiffness, and viscoelasticity of the gels were improved by the treatments. Among them, the modification effect of 0.24% (w/v) EGCG was the most prominent. Through the analysis of microstructure and composition, it was found to be due to the covalent addition, disulfide bond formation, etc., between the quinone derivatives of phenolic acids and the side chains of nucleophilic amino acids. Phenolic acid modification of GSPI may be a potential ingredient strategy in its processing.

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Section: Introductionmentioning

confidence: 99%

Alkali-Induced Phenolic Acid Oxidation Enhanced Gelation of Ginkgo Seed Protein

Zhang

Liu

Zhao

et al. 2023

Foods

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“…Although carbonylation of MP was ascribed to ROS, especially HO · , − other radicals, such as protein radicals, may also be involved. − To verify the primary role of HO · in MP carbonylation with experimental evidence, we spiked methanol (MeOH) in the MP samples containing Fenton reagents and various amounts of GA. Figure d shows that the MeOH, a well-established scavenger of HO · , completely quenched MP carbonylation by Fenton reagents and GA. This experiment provided solid evidence for the hypothesis that HO · radicals are the primary oxidant, resulting in MP carbonylation.…”

Section: Resultsmentioning

confidence: 99%

Mechanistic Insights into Myofibrillar Protein Oxidation by Fenton Chemistry Regulated by Gallic Acid

Wang

et al. 2023

J. Agric. Food Chem.

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Gallic acid (GA, 3,4,5-trihydroxybenzoic acid) is a widely used natural food additive of interest to food chemistry researchers, especially regarding its effects on myofibrillar protein (MP) oxidation. However, existing studies regarding MP oxidation by GA-combined with Fenton reagents are inconsistent, and the detailed mechanisms have not been fully elucidated. This work validated hydroxyl radical (HO • ) as the primary oxidant for MP carbonylation; in addition, it revealed three functions of GA in the Fenton oxidation of MP. By coordination with Fe(III), GA reduces Fe(III) to generate Fe(II), which is the critical reagent for HO • generation; meanwhile, the coordination improves the availability and reactivity of Fe(III) under weakly acidic and near-neutral pH, i.e., pH 4−6. Second, the intermediates formed during GA oxidation, including semiquinone and quinone, promoted Fenton reactivity by accelerating Fe catalytic cycling. Finally, GA can scavenge HO • radicals, thus exhibiting a certain degree of antioxidant property. All three functions contribute to MP oxidation as observed in GA-containing meat.

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“…However, higher β-sheet content might induce poor gel water retention. Cheng et al [32] found that the caffeic acid-modified myofibril gel had the most β-sheet content, but the gel water retention was poor. The changes in the α-helix and β-sheet contents of the gel structure were attributed to ultrasonic cavitation forces.…”

Section: Resultsmentioning

confidence: 99%