Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein

Cao, Yungang; Xiong, Youling L.

doi:10.1016/j.foodchem.2015.02.036

Cited by 436 publications

(272 citation statements)

References 39 publications

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“…Interaction with the phenolic derivatives ostensibly resulted in a destabilization of the β‐Lg structure through the disruption of intramolecular hydrophobic and electrostatic forces. Such phenolic‐induced structural destabilization of protein has been documented in previous studies (Cao and Xiong ; Tang and others ). However, Ali and others () reported that chlorogenic acid‐modified β‐Lg (at pH 9.0) was thermally more stable.…”

Section: Resultssupporting

confidence: 74%

Interaction of Whey Proteins with Phenolic Derivatives Under Neutral and Acidic pH Conditions

Cao

Xiong

2017

Journal of Food Science

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167

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Integration of gallic acid (GA) and its derivative epigallocatechin gallate (EGCG; 20, 120, and 240 μmol/g, protein basis) into whey protein isolate (WPI) at room temperature and pH 3.0 and pH 7.0 was investigated. At pH 7.0, both phenolics caused significant structural changes and EGCG induced greater digestibility of WPI. Total sulfhydryl in WPI decreased from 28.6 to 7.6 μmol/g and surface hydrophobicity declined by nearly 50% with 240 μmol/g EGCG at pH 7.0. Similar but less appreciable changes were produced by GA and at pH 3.0. Isothermal titration and fluorescence quenching tests showed moderately weak binding of WPI with GA but strong binding with EGCG at pH 7.0. Both phenolics at high concentrations lowered the thermal transition temperature of β-lactoglobulin by 0.5 °C to 1.4 °C and promoted its digestion. The phenolics also displayed a remarkable synergism with peptides in the WPI digest exerting radical scavenging activity.

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Section: Resultssupporting

confidence: 74%

Interaction of Whey Proteins with Phenolic Derivatives Under Neutral and Acidic pH Conditions

Cao

Xiong

2017

Journal of Food Science

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167

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“…The intrinsic fluorescence spectra of protein are due to their aromatic amino acid residues, particularly the tryptophan residues (Jia et al ., ). When tryptophan residues were buried in the centre of the protein, a high fluorescence intensity usually appeared than exposing to the surface of a protein (Cao & Xiong, ). As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Effects of hydroxyl radical induced oxidation on water holding capacity and protein structure of jumbo squid (Dosidicus gigas) mantle

Zhu

Hai-zhen

et al. 2019

Int J of Food Sci Tech

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Summary Protein oxidation is considered as an important issue in food preservation process. In the present study, the potential influence of protein oxidation on water holding capacity and protein structure of jumbo squid (Dosidicus gigas) mantle was investigated. After the hydroxyl radical oxidation, it was found that the carbonyl, surface hydrophobicity and dityrosine content of myofibrillar protein significantly increased (P < 0.05), while the content of total sulphydryl decreased significantly (P < 0.01). Meanwhile, the fluorescence intensity of squid was weakened, and the maximum absorption peak of fluorescence red shift as the H2O2 concentration increased. The sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) showed that not only the protein cross‐linking but also degradation could have occurred. The content of α‐helix decreased, the content of β‐sheet, β‐turn and the unordered structures increased after oxidation. In addition, oxidation resulted in a decrease in water holding capacity. Taken together, oxidation resulted in the damage of the myofibrillar structure, the increase in muscle loss rate and the decrease in water holding capacity.

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“…Generally, in the folded state, tryptophan residues are located within the core (a hydrophobic environment) of the protein, having a high quantum yield and therefore high fluorescence intensity [27]. While in an unfolded state, they tend to expose to solvent, leading to reduced fluorescence intensity.…”

Section: Tryptophan Fluorescencementioning

confidence: 99%

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

et al. 2016

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Oxidation extent of myofibrillar protein (MP) from silver carp (Hypophthalmichthys molitrix) was affected by the content and type of lipid peroxidation (LPO) products. Oxidized linoleic acid (OLA) was selected as a main representative of lipid peroxidation to investigate the effects of oxidative modification of LPO products on MP structure. Structural changes of the oxidized myofibrillar protein were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. Heating procedure was also applied for further evaluation of gelling properties. The results from SDS-PAGE indicated that aggregation and denaturation of myosin occurred in the oxidized system. The presence of OLA intensified oxidation-initiated loss of a-helix conformation as well as tertiary structure of MP. With the addition of OLA concentration less than 3 mM, a remarkably enhanced gelling capacity of MP was observed. While the excessive covalent bond (OLA > 5 mM) could lead to the breakage of protein-protein bonds, causing the collapse of the gel structure. The gelation procedure induced by OLA involved simultaneous protein oxidation and internal cross-linking.

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Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein

Cited by 436 publications

References 39 publications

Interaction of Whey Proteins with Phenolic Derivatives Under Neutral and Acidic pH Conditions

Interaction of Whey Proteins with Phenolic Derivatives Under Neutral and Acidic pH Conditions

Effects of hydroxyl radical induced oxidation on water holding capacity and protein structure of jumbo squid (Dosidicus gigas) mantle

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

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