Dose-dependent effects of rosmarinic acid on formation of oxidatively stressed myofibrillar protein emulsion gel at different NaCl concentrations

Wang, Shuangxi; Zhang, Yumeng; Chen, Lin; Xu, Xinglian; Li, Zhixi; Feng, Xianchao

doi:10.1016/j.foodchem.2017.09.114

Cited by 101 publications

(72 citation statements)

References 32 publications

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“…As for the existence of unrecovered polymers non-disulfide bonds, such as dityrosine, carbonyl–NH 2 , and other covalent linkages, which data can link to the data of sulfhydryl, free amines and dityrosine. This was similar to the report of Shuangxi et al [23], who found that rosmarinic acid (60 and 300 μM/g) accelerated MP polymerization and that the reduction in MHC intensity was due to the formation of quinone–thiol and amine–quinone adducts.…”

Section: Resultssupporting

confidence: 92%

Effect of Chlorogenic Acid on the Physicochemical and Functional Properties of Coregonus Peled Myofibrillar Protein through Hydroxyl Radical Oxidation

et al. 2019

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The effects of chlorogenic acid (CA) (6, 30, and 150 μM/g protein) on the physicochemical and functional properties of Coregonus peled myofibrillar protein (MP) through oxidation using a hydroxyl radical oxidation system (0.01 mM FeCl3, 0.01 mM Asc, and 1 mM H2O2) were investigated. The result showed that CA inhibited the increase in protein carbonyl content but did not prevent losses in sulfhydryl and free amine contents caused by oxidation. The presence of CA also increased conformational changes in the secondary and tertiary structures of oxidized MP. Oxidized MP containing 6 μM/g CA had superior functional properties (solubility, emulsifying, foaming, and gel properties), while oxidized MP containing 150 μM/g CA aggregated, resulting in insolubility and a poor gel network.

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Section: Resultssupporting

confidence: 92%

Effect of Chlorogenic Acid on the Physicochemical and Functional Properties of Coregonus Peled Myofibrillar Protein through Hydroxyl Radical Oxidation

et al. 2019

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“…Epicatechin was oxidized into a quinine derivative in this oxidation system. This study was in accordance with those previous reports in which phenolic compounds inhibited protein carbonyl content, such as quercetin [27] ，rosmarinic acid [28] and EGCG. [29,30] Total and free sulfydryl groups MP is rich in sulfydryl groups, which are susceptible to attack by reactive oxygen species and can then convert to intra-and intermolecular disulfide bond linkages.…”

Section: Carbonyl Contentsupporting

confidence: 94%

Protective effects of epicatechin on the oxidation and N-nitrosamine formation of oxidatively stressed myofibrillar protein

Ling

2019

International Journal of Food Properties

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The present study investigated the protective effects of the polyphenol epicatechin on the protein structural changes, gel properties and N-nitrosodiethylamine (NDEA) formation of oxidatively stressed myofibrillar protein (MP). Results showed that oxidation treatments to MP significantly increased their carbonyl content and surface hydrophobicity as compared to the control groups (p < 0.05). Epicatechin inhibited protein carbonyl content and surface hydrophobicity, especially treated with 2 mM epicatechin. Under oxidative conditions, the fluorescence intensity of tryptophan gradually decreased with the increase of epicatechin concentrations from 0 to 2 mM. The storage modulus (G') was increased gradually after oxidation and epicatechin treatment. Epicatechin reduced the loss of P 22 and water holding capacity (WHC), promoted the hydration of the proteins. Under oxidative conditions, epicatechin had a concentration dependent effect on the formation of NDEA; low concentrations of epicatechin promoted NDEA formation, while high concentrations inhibited NDEA production. In conclusion, an appropriate quantity of polyphenols can inhibit the oxidation of MP and formation of N-nitrosamines. ARTICLE HISTORY

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“…Myofibrillar protein is a major component of muscle protein and has a significant effect on the processing and manufacturing of meat products [ 9 ]. Myofibrillar protein is a salt-soluble protein that is known to denature during thermal processing to form a gel [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

Effect of Interaction between Mealworm Protein and Myofibrillar Protein on the Rheological Properties and Thermal Stability of the Prepared Emulsion Systems

Kim

Lee

Yong

et al. 2020

Foods

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In this study, we investigated the effect of replacing myofibrillar protein (pork ham) with edible insect proteins (Tenebrio molitor L.) in meat emulsion systems and examined the interaction between the two types of proteins. We also evaluated the rheological properties and thermal stability of these meat emulsions. The replacement ratios of myofibrillar protein and edible insect protein were as follows: 100:0 (EI0), 80:20 (EI20), 60:40 (EI40), 40:60 (EI60), 20:80 (EI80), and 0:100 (EI100). The pH, redness, and yellowness of the emulsion systems, after replacing myofibrillar protein with T. molitor protein, significantly increased with T. molitor protein concentrations. In contrast, the lightness, hardness, cohesiveness, gumminess, chewiness, apparent viscosity, and differential scanning calorimetry (DSC) of the emulsion systems decreased significantly with increasing T. molitor protein concentrations. The backscattering values of EI0, EI20, and EI40 decreased evenly in all spots of the dispersions as the storage time increased. Thus, up to 40% of pork myofibrillar protein could be replaced with T. molitor protein in meat emulsion systems. The results also suggest that the interaction between edible insect protein and myofibrillar protein degrades the rheological properties and thermal stability of the meat emulsion systems.

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Dose-dependent effects of rosmarinic acid on formation of oxidatively stressed myofibrillar protein emulsion gel at different NaCl concentrations

Cited by 101 publications

References 32 publications

Effect of Chlorogenic Acid on the Physicochemical and Functional Properties of Coregonus Peled Myofibrillar Protein through Hydroxyl Radical Oxidation

Effect of Chlorogenic Acid on the Physicochemical and Functional Properties of Coregonus Peled Myofibrillar Protein through Hydroxyl Radical Oxidation

Protective effects of epicatechin on the oxidation and N-nitrosamine formation of oxidatively stressed myofibrillar protein

Effect of Interaction between Mealworm Protein and Myofibrillar Protein on the Rheological Properties and Thermal Stability of the Prepared Emulsion Systems

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