pH-Dependent complexation between β-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study

Chen, Lu; Lu, Yingcong; Liu, Jia; Zhao, Ru; Sun, Yonghai; Sun, Boyang; Wang, Cuina

doi:10.1016/j.foodchem.2021.130230

Cited by 39 publications

(11 citation statements)

References 50 publications

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“…A fluorescence quenching experiment was applied to explore the binding parameters between WPC-HMP and CA or RA because all major components of WPC contain tryptophan and tyrosine, which possess intrinsic fluorescence. As shown in Figure 2, upon excitation at 280 nm, WPC-HMP showed a maximum emission wavelength at 330 to 334 nm for all pH values, and a slight redshift peak position was observed after phenolic acid addition, conveying a change in the tertiary structure of the protein and transfer of the fluorophore from hydrophobic to a more hydrophilic environment (Wang et al, 2021a). Concurrently, both phenolic acids regularly quenched the fluorescence intensity of WPC at an excitation wavelength of 280 nm (Wang et al, 2016).…”

Section: Binding Ability Of Wpc-hmp To Ca or Ramentioning

confidence: 84%

Formation and characterization of noncovalent ternary complexes based on whey protein concentrate, high methoxyl pectin, and phenolic acid

Zhang

Yang

et al. 2022

Journal of Dairy Science

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Protein-polysaccharide-polyphenol noncovalent ternary complexes possess unique physicochemical, structural, and functional properties. In the present study, ternary complexes based on whey protein concentrate (WPC; 2%, wt/vol) and high methoxyl pectin (HMP; 0.5%, wt/vol) complexes and 0.2 to 0.6% (wt/vol) chlorogenic acid (CA) or rosmarinic acid (RA) were formed and characterized at 3 pH values (4, 4.5, and 5). The pH conditions were decided according to phase diagram of WPC and HMP during acidification. Fluorescence quenching experiments indicated that WPC-HMP complexes bound RA stronger than CA and the binding constant increased with increasing pH for both phenolic acids. Particle size of ternary complexes decreased and absolute ζ-potential increased with pH values changing from 4 to 5, and RA influenced the particle size of WPC-HMP complexes greater than CA. The CA and RA in ternary complexes showed good stability against UV light with pH order of pH 5 > pH 4.5 > pH 4. Fourier-transform infrared spectroscopy spectra indicated the involvement of hydrogen bonding between WPC-HMP and CA or RA. Antibacterial tests showed that ternary complexes had good antibacterial activity against Staphylococcus aureus and Escherichia coli at concentrations of 6.2 mg/mL and the ability increased with decreasing pH values. All ternary complexes possessed strong scavenging radical capacities with median inhibitory concentration (IC 50 ) values ranging from 2.71 ± 0.05 to 6.20 ± 0.41 μg/mL. Antioxidative ability of ternary complexes increased as pH went up and WPC-HMP-RA showed significantly higher antioxidative property compared with WPC-HMP-CA. Data may provide useful information for rational design of ternary complexes and applications of the formed complexes in food matrices such as beverages and emulsions.

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Section: Binding Ability Of Wpc-hmp To Ca or Ramentioning

confidence: 84%

Formation and characterization of noncovalent ternary complexes based on whey protein concentrate, high methoxyl pectin, and phenolic acid

Zhang

Yang

et al. 2022

Journal of Dairy Science

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“…Heating could change the movement rate of amino acids and the spatial structure of proteins, and molecular dynamics simulation (MDs) is often used to study the movement vector, as well as the structure changes at the molecular level (Wang et al, 2021; Yu et al, 2021). MDs of β ‐Lg were performed at 298 K, 318 K, 338 K, 358 K, and 373 K for 100 ns each, and root‐mean‐square deviation (RMSD) was calculated to determine the system equilibrium status.…”

Section: Resultsmentioning

confidence: 99%

Effects of preheating temperatures on β‐lactoglobulin structure and binding interaction with dihydromyricetin

Zhang

Guan

Huang

et al. 2022

eFood

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Low aqueous solubility limits the bioactivity and bioaccessibility of dihydromyricetin (DHM). Preheating treatment affects the loading efficiency of β-lactoglobulin (β-Lg) to polyphenols, but the mechanism remained unclear. In this study, a serial of temperatures (298 K, 318 K, 338 K, 358 K, and 373 K) were set to analyze the preheating effects on the loading efficiency of β-Lg to DHM, and secondary structure change, binding interactions, and particle size distribution were measured and compared with discover the effects. β-Lg preheated at 358 K possessed the highest binding percentage of 0.45, higher than 0.27, 0.30, 0.36, and 0.40 at 298 K, 318 K, 338 K, and 373 K, the exposure of inside hydrophobic residues contribute the hydrophobic interaction with DHM. Fluorescence quenching and molecular docking analysis showed that DHM tend to bind to β-Lg preheated at 358 K with a binding constant of 1.76 × 10 5 L mol −1 and a binding score of −5.84 kcal mol −1 , higher than that of other temperatures. Particle size distribution showed that Z-average size at 358 K was 16.34 nm, significantly higher than others of 7.64, 8.06, 6.84, and 13.4 nm. Preheating unfolded the structure of β-Lg, exposing the internal residues and enhancing the interaction with DHM.

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“…Native β-LG showed maximum emission intensity at a wavelength of $334 nm, similar to previous studies. [4,26] The peak was shifted to 335 nm after ultrasound pretreatment, which was indicative of Trp residues in β-LG moving to a more polar region, and suggesting a slight tertiary structure change in β-LG induced by ultrasound. [26,27] Similar results of a small red shift of β-LG induced by ultrasound have been reported in the literature.…”

Section: Effects Of Resveratrol On Fluorescence Spectra Of Native And...mentioning

confidence: 99%

Towards understanding the interaction between ultrasound‐pretreated β‐lactoglobulin monomer with resveratrol

et al. 2022

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Increasingly, studies are using ultrasound to elevate the functional properties of proteins, so the interaction between phenolic compounds and proteins induced by ultrasound needs to be further understood. β-Lactoglobulin (β-LG) at pH 8.1, which exists mainly as monomers, was ultrasound treated at 20 kHz ultrasonic intensity and 30% amplitude for 0-5 min and subsequently interacted with resveratrol. Fluorescence data showed that ultrasound pretreatment improved binding constant (K a ) from (1.62 ± 0.45) Â 10 5 to (9.43 ± 0.55) Â 10 5 M À1 and binding number from 1.13 ± 0.09 to 1.28 ± 0.11 in a static quenching mode. Fluorescence resonance energy transfer (FRET) analysis indicated that resveratrol bound to the surface hydrophobic pocket of native and treated proteins with no obvious changes in energy transfer efficiency (E) and Föster's distance (r). Thermodynamic parameters indicated that ultrasonication shifted the main driving force from the hydrophobic force for native and 1-min treated β-LG to van der Waals forces and hydrogen bonding for both 3-min and 5-min treated proteins. Ultrasonication and resveratrol addition generated significant differences in surface hydrophobicity and the surface charge of the protein (P < 0.05), whereas they had little influence on the secondary structure of β-LG.Compared with the native β-LG/resveratrol complex, ultrasound-treated protein complexes showed significantly stronger 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) scavenging capacity (P < 0.05), and kept relatively stable after 180-min irradiation. Data provided by this study can lead to a better comprehension of the structure and molecular events occurring during the complexing process between an ultrasound-pretreated protein with polyphenol.

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pH-Dependent complexation between β-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study

Cited by 39 publications

References 50 publications

Formation and characterization of noncovalent ternary complexes based on whey protein concentrate, high methoxyl pectin, and phenolic acid

Formation and characterization of noncovalent ternary complexes based on whey protein concentrate, high methoxyl pectin, and phenolic acid

Effects of preheating temperatures on β‐lactoglobulin structure and binding interaction with dihydromyricetin

Towards understanding the interaction between ultrasound‐pretreated β‐lactoglobulin monomer with resveratrol

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