Changes in the structural and gel properties of pork myofibrillar protein induced by catechin modification

Jia, Ning; Wang, Letian; Li, Mohan; Liu, Dengyong; Kong, Baohua

doi:10.1016/j.meatsci.2017.01.004

Cited by 146 publications

(83 citation statements)

References 40 publications

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“…Addition of green tea extract (as seen for the 25–375 ppm concentration interval of phenolic compounds) to meat emulsions showed that heat treatment (70 ° for 15 min) depleted thiols in a dose-dependent manner, and it was suggested, that the excessive loss of thiols predominantly was caused by thiol-quinone adduct formation [ 14 ]. Likewise, recent studies by other groups have demonstrated that addition of chlorogenic acid [ 34 ], catechin [ 35 ], or (-)-epigallocatechin-3-gallate (EGCG) [ 36 ] to myofibrillar proteins change the physicochemical properties of the proteins, especially the gelling properties. The changes are found to be either advantageous or detrimental depending on the concentration applied, and all mentioned studies assign the changes to be caused by the formation of quinone-protein covalent interactions.…”

Section: Resultsmentioning

confidence: 99%

Dose-Dependent Effects of Green Tea or Maté Extracts on Lipid and Protein Oxidation in Brine-Injected Retail-Packed Pork Chops

2018

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Background: Phenolic plant extracts are added as antioxidants in meat to prevent lipid oxidation, but depending on the concentration applied, may affect proteins either through covalent interactions or by serving as a prooxidant. Methods: Brine-injected pork chops prepared with green tea extract (25–160 ppm gallic acid equivalents (GAE)), or maté extract (25–160 ppm GAE) and stored (5 °C, 7 days) in high-oxygen atmosphere packaging (MAP: 80% O2 and 20% CO2) were analyzed for color changes, lipid oxidation by thiobarbituric acid reactive substances (TBARS), and protein oxidation evaluated by thiol loss and protein radical formation by electron spin resonance (ESR) spectroscopy, and compared to a control without antioxidant. Results: Extract of maté and green tea showed significant and comparable antioxidative effects against formation of TBARS in brine-injected pork chops for all concentrations applied compared to the control. Protein radical formation decreased significantly by addition of 25 ppm maté extract, but increased significantly by addition of 80–160 ppm green tea extract, when monitored as formation of protein radicals. Meanwhile, protein thiol groups disappeared when applying the extracts by reactions assigned to addition reactions of oxidized phenols from the extracts to protein thiols. Conclusion: Maté is accordingly a good source of antioxidants for protection of both lipids and proteins in brine-injected pork chops chill-stored in high-oxygen atmosphere, though the dose must be carefully selected.

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Section: Resultsmentioning

confidence: 99%

Dose-Dependent Effects of Green Tea or Maté Extracts on Lipid and Protein Oxidation in Brine-Injected Retail-Packed Pork Chops

2018

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“…The initial carbonyl content was 0.6 nmol/mg before oxidation, whereas it increased to 1.31 nmol/mg after 12 hr of oxidation. However, the addition of TP/HP‐β‐CD lowered the carbonyl content of oxidized MPs most likely by scavenging free radicals and chelating metal ions (Jia, Wang, Shao, Liu, & Kong, 2017). Research by Zhang, Chen, Lv, Wang, and Feng (2018) showed that β‐cyclodextrins were used to reduce covalent and noncovalent interactions between epigallocatechin‐3‐gallate (EGCG) and MPs under oxidative stress, which prevented the increase of carbonyl content and the unfolding of MPs caused by EGCG, as well the structural stability and solubility were improved significantly.…”

Section: Resultsmentioning

confidence: 99%

“…MPs are rich in SH groups, which are easily attacked by oxidative inducers and converted into intramolecular or intermolecular disulfide bonds, thus causing protein cross‐linking polymerization (Jia et al., 2017). Therefore, lower SH content is an important indicator of protein oxidation.…”

Section: Resultsmentioning

confidence: 99%

Inclusion complexes of tea polyphenols with HP‐β‐cyclodextrin:Preparation, characterization, molecular docking, and antioxidant activity

Zhong

Lidan

et al. 2020

Journal of Food Science

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The purpose of this study was to prepare and characterize inclusion complexes between tea polyphenol (TP) and hydroxypropyl-β-cyclodextrin (HP-β-CD), and to evaluate their antioxidant properties. Freeze-drying was used to prepare the inclusion complex of TP/HP-β-CD at different component ratios (1:0.5, 1:1, and 1:2). The supermolecular structure of the TP/HP-β-CD complex was characterized by Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), and scanning electron microscopy (SEM). Molecular docking was used to simulate the positions and interactions of the binding sites of TP/HP-β-CD inclusion complexes and target protein receptors. In addition, the effects of TP/HP-β-CD inclusion complexes on myofibrillar protein (MP) from lamb tripe were observed under oxidative conditions. Results showed that TP was encapsulated in the cavity of HP-β-CD to form an optimal complex with 1:2 molar ratio of stoichiometry, while the FTIR, TGA, and SEM studies also support the inclusion process. Molecular modeling results were systematically analyzed to determine the stability of inclusion complexes and protein. Furthermore, the addition of an appropriate concentration (5 to 105 µmol/g) of TP/HP-β-CD inclusion complex decreased the carbonyl content, hydrophobicity, and protein aggregation of MP from lamb tripe, whereas it increased the sulfhydryl content. This improved antioxidant activity and bioavailability of the inclusion complexes will be beneficial for its potential applications in food.Practical Application: Tea polyphenol was an antioxidant with potential for the field of food. In this study, the unstable properties of tea polyphenols were evaluated and were improved by inclusion of HP-β-cyclodextrin. The binding mode of the inclusion complex with protein was revealed via the molecular docking method, and the application of inclusion complex to control protein oxidation was studied. Results showed that the inclusion complex could effectively inhibit protein oxidation, which can provide a reference for the application of polyphenols in meat products and the improvement of protein properties.

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“…Surface hydrophobicity is widely applied to evaluate the extent of hydrophobic amino acid residues distributed on protein surfaces (Jia et al, 2017). Hydrophobic BPB probes, such as 8-anilinonaphthalene-1-sulfonic acid, can strongly bind to proteins via hydrophobic interactions, and binding strength is a suitable parameter to reflect protein hydrophobicity (Chelh et al, 2006;Cao et al, 2015).…”

Section: Changes In Surface Hydrophobicitymentioning

confidence: 99%

“…With the formation of protein cross-linking, protein polymers are subsequently generated (Lund et al, 2011). Jia et al (2017) suggested that the exposure of hydrophobic areas is necessary to generate large protein polymers. A high hydrophobic interaction between proteins can promote protein aggregation via intermolecular acting forces (Sun et al, 2013).…”

Section: Sds-page Analysismentioning

confidence: 99%

Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

Wang

Gan

et al. 2018

Int J of Food Sci Tech

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Summary We investigated the effect of peroxyl radicals (ROO·), which are products of lipid peroxidation, on the structure and gel properties of myofibrillar proteins (MPs) isolated from rabbit meat. 2,2′‐Azobis(2‐amidinopropane) dihydrochloride (AAPH) was heated to stably derive ROO·. As the AAPH concentration increased, the protein carbonyl compounds significantly accumulated (P < 0.05), and the total sulfhydryl content was significantly lost (P < 0.05). Circular dichroism spectra, UV absorption spectra, intrinsic fluorescence spectra and surface hydrophobicity revealed that ROO· caused protein unfolding and conformational changes in MPs. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) analysis indicated that moderate (0–3 mm) and relatively high (5 and 10 mm) AAPH concentrations could lead to protein crosslinking and protein aggregation, respectively. These changes in protein structure could influence the gelling properties of MPs. Low‐level protein oxidation could increase gel strength and water holding capacity, whereas high‐level protein oxidation could reduce gel properties.

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Changes in the structural and gel properties of pork myofibrillar protein induced by catechin modification

Cited by 146 publications

References 40 publications

Dose-Dependent Effects of Green Tea or Maté Extracts on Lipid and Protein Oxidation in Brine-Injected Retail-Packed Pork Chops

Dose-Dependent Effects of Green Tea or Maté Extracts on Lipid and Protein Oxidation in Brine-Injected Retail-Packed Pork Chops

Inclusion complexes of tea polyphenols with HP‐β‐cyclodextrin:Preparation, characterization, molecular docking, and antioxidant activity

Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

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