Effect of thermal treatment on the molecular-level interactions and antioxidant activities in β-casein and chlorogenic acid complexes

Yin, Zhucheng; Qie, Xuejiao; Zeng, Maomao; Wang, Zhaojun; Qin, Fang; Chen, Jie; Li, Weiwei; He, Zhiyong

doi:10.1016/j.foodhyd.2021.107177

Cited by 29 publications

(12 citation statements)

References 47 publications

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“…The K sv and K q values were obtained from the Stern–Volmer equation (Fig. 5(f)), and the Stern–Volmer curves of DLp–( E , E )‐2,4‐heptadienal complex exhibited a linear relationship and all the estimated K q values were higher than the maximum collisional quenching constant, being 2.0 × 10 10 L mol −1 S −1 , thus confirming that the quenching mechanism was dominated by static quenching due to the presence of a non‐luminescent complex between DLp and ( E , E )‐2,4‐heptadienal 54 …”

Section: Resultsmentioning

confidence: 73%

“…5(f)), and the Stern-Volmer curves of DLp-(E,E)-2,4-heptadienal complex exhibited a linear relationship and all the estimated K q values were higher than the maximum collisional quenching constant, being 2.0 × 10 10 L mol −1 S −1 , thus confirming that the quenching mechanism was dominated by static quenching due to the presence of a nonluminescent complex between DLp and (E,E)-2,4-heptadienal. 54 The quenching constants (K sv ) of DLp for (E,E)-2,4-heptadienal for the untreated, heated (65/100 °C) and UHP-pretreated (100/ 500 MPa for 10 min) samples were 2.006 × 10 4 , 2.283 × 10 4 , 1.058 × 10 4 , 0.927 × 10 4 and 1.020 × 10 4 L mol −1 , respectively. The relatively high quenching constants of the untreated group may be due to attractive electrostatic forces generated by positively charged groups around accessible tryptophan residues, with lower quenching constants after treatments indicating that the tryptophan residues were concealed and electrostatic forces were disrupted by thermal and pressurization processes.…”

Section: Microstructural Observations Using Semmentioning

confidence: 94%

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Contribution of process‐induced molten‐globule state formation in duck liver protein to the enhanced binding ability of (E,E)‐2,4‐heptadienal

Han

Zheng²,

Wang

et al. 2023

J Sci Food Agric

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BACKGROUND Extracted proteins of alternative animal origin tend to present strong off‐flavor perception due to physicochemical interactions of coextracted off‐flavor compounds with proteins. To investigate the relationship between absorption behaviors of volatile aromas and the processes‐induced variations in protein microstructures and molecular conformations, duck liver protein isolate (DLp) was subjected to heating (65/100 °C, 15 min) and ultra‐high pressure (UHP, 100–500 MPa/10 min, 28 °C) treatments to obtain differential unfolded protein states. RESULTS Heat and UHP treatments induced the unfolding of DLp to varied degrees, as revealed by fluorescence spectroscopy, ultraviolet–visible absorption, circular dichroism spectra and surface hydrophobicity measurements. Two types of heating‐denatured states with varied unfolding degrees were obtained, while UHP at both levels of 100/500 MPa caused partial unfolding of DLp and the presence of a molten‐globule state, which significantly enhanced the binding affinity between DLp and (E,E)‐2,4‐heptadienal. In particular, significantly modified secondary structures of DLp were observed in heating‐denatured samples. Excessive denaturing and unfolding degrees resulted in no significant changes in the absorption behavior of the volatile ligand, as characterized by observations of fluorescence quenching and analysis of headspace concentrations. CONCLUSION Defining process‐induced conformational transition behavior of matrix proteins could be a promising strategy to regulate food flavor attributes and, particularly, to produce DLp coextracted with limited off‐flavor components by modifying their interaction during extraction processes. © 2023 Society of Chemical Industry.

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Section: Resultsmentioning

confidence: 73%

Section: Microstructural Observations Using Semmentioning

confidence: 94%

Contribution of process‐induced molten‐globule state formation in duck liver protein to the enhanced binding ability of (E,E)‐2,4‐heptadienal

Han

Zheng²,

Wang

et al. 2023

J Sci Food Agric

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“…When excited at 280 nm, amino acids with Phenyl rings such as tryptophan (Trp), tyrosine (Tyr), and phenylalanine (Phe) cause the intrinsic fluorescence of the protein. 25 The β-CN contains one tryptophan Trp-143 with an intrinsic fluorescence, when other molecules interact with casein, tryptophan fluorescent can change based on the effect of such…”

Section: Resultsmentioning

confidence: 99%

Binding of β-casein with fluvastatin and pitavastatin

Dezhampanah

Rajabi

2022

JSCS

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In this work, the binding interaction of fluvastatin (FLU) and pitavastatin (PIT) with bovine ?-casein (?-CN) were performed under physiological conditions (pH 7.2) by fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR) and molecular docking methods. Due to the formation of FLU-?-CN and PIT-?-CN complexes, the intrinsic fluorescence of ?-CN was quenched. The number of bound FLU and PIT per protein molecule (n) were about 1, also the binding constant of FLU-?-CN and PIT-?-CN complexes were 7.96?104 and 3.44?104M-1 at 298 K, respectively. This result suggests that the binding affinity of FLU to ?-CN was higher than that for PIT. Molecular modeling showed different binding sites for FLU and PIT on ?-CN. All these experimental results suggest that ?.

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“…The ferric ion-reducing antioxidant power (FRAP) method is widely used to determine the antioxidant activity indirectly (i.e., the ability of the tested substance to reduce ferric iron to ferrous iron) [ 80 ]. Yin et al [ 60 ] found that after β-casein was combined with chlorogenic acid, the FRAP value of the complex was significantly higher than the sum of β-casein alone and chlorogenic acid alone, indicating a synergistic effect. Another report showed that the FRAP values of chlorogenic acid in the presence of β-lactoglobulin were significantly increased at high temperatures (85–121 °C) compared to the values of chlorogenic acid alone [ 61 ].…”

Section: Assessment Of Antioxidant Properties Of Polyphenol–protein C...mentioning

confidence: 99%

Molecular Mechanisms and Applications of Polyphenol-Protein Complexes with Antioxidant Properties: A Review

Feng

Jin

et al. 2023

Antioxidants

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Proteins have been extensively studied for their outstanding functional properties, while polyphenols have been shown to possess biological activities such as antioxidant properties. There is increasing clarity about the enhanced functional properties as well as the potential application prospects for the polyphenol–protein complexes with antioxidant properties. It is both a means of protein modification to provide enhanced antioxidant capacity and a way to deliver or protect polyphenols from degradation. This review shows that polyphenol–protein complexes could be formed via non-covalent or covalent interactions. The methods to assess the complex’s antioxidant capacity, including scavenging free radicals and preventing lipid peroxidation, are summarized. The combination mode, the type of protein or polyphenol, and the external conditions will be the factors affecting the antioxidant properties of the complexes. There are several food systems that can benefit from the enhanced antioxidant properties of polyphenol–protein complexes, including emulsions, gels, packaging films, and bioactive substance delivery systems. Further validation of the cellular and in vivo safety of the complexes and further expansion of the types and sources of proteins and polyphenols for forming complexes are urgently needed to be addressed. The review will provide effective information for expanding applications of proteins and polyphenols in the food industry.

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Effect of thermal treatment on the molecular-level interactions and antioxidant activities in β-casein and chlorogenic acid complexes

Cited by 29 publications

References 47 publications

Contribution of process‐induced molten‐globule state formation in duck liver protein to the enhanced binding ability of (E,E)‐2,4‐heptadienal

Contribution of process‐induced molten‐globule state formation in duck liver protein to the enhanced binding ability of (E,E)‐2,4‐heptadienal

Binding of β-casein with fluvastatin and pitavastatin

Molecular Mechanisms and Applications of Polyphenol-Protein Complexes with Antioxidant Properties: A Review

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