Combined spectroscopic, molecular docking and quantum mechanics study of β-casein and ferulic acid interactions following UHT-like treatment

Condict, Lloyd; Kaur, Jasmeet; Hung, Andrew; Ashton, John; Kasapis, Stefan

doi:10.1016/j.foodhyd.2018.10.055

Cited by 55 publications

(21 citation statements)

References 39 publications

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“…The peaks in the range of 1075.91–1449.75 cm –1 corresponding to the N–H groups (amide I) in the native WPI shifted in the WPI-EGCG-LA spectra due to the incorporation of EGCG. This indicates that the WPI is bound to EGCG through CO, C–N, and N–H groups, revealing a change in the protein secondary structure . Moreover, the absence of the peak 1158.82 cm –1 of the native WPI from the WPI-EGCG-LA spectra was attributed to the interactions of the wall materials.…”

Section: Resultsmentioning

confidence: 94%

Enhanced In Vitro Functionality and Food Application of Lactobacillus acidophilus Encapsulated in a Whey Protein Isolate and (−)-Epigallocatechin-3-Gallate Conjugate

Bora

Lü

et al. 2021

J. Agric. Food Chem.

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The present study investigated the potential of free radical grafting conjugation of whey protein isolate (WPI) and (−)-epigallocatechin-3-gallate (EGCG), followed by freeze-drying, for the safe delivery of probiotic Lactobacillus acidophilus (LA) upon digestion and in food systems. WPI-EGCG-LA microspheres presented higher encapsulation efficiency (97%) than native WPI-LA (70%) and maltodextrin (MD-LA 75%). The physicochemical characteristics of all microspheres, including moisture content, water activity, and hygroscopicity, were within the acceptable range for the stability of industrial powders. Scanning electron microscopy of WPI-EGCG-LA revealed a glass-like structure, with a smoother and less porous surface area than WPI-LA and MD-LA, as a result of the strong binding affinity between WPIs and EGCG. Particle sizes ranged from 438.4 to 453.3 μm. The structural stability of WPI-EGCG-LA was further confirmed by Fourier transform infrared spectra, which revealed some changes in the protein secondary structure. Thermogravimetric and differential scanning calorimetry analysis showed that WPI-EGCG conjugates had higher thermal stability than native WPIs and MD. Additionally, cells encapsulated in WPI-EGCG conjugates demonstrated higher in vitro survivability and surface hydrophobicity compared to free or WPI-and MD-encapsulated cells. Furthermore, WPI-EGCG-LA microspheres exerted enhanced in vitro antioxidant (78%) and antidiabetic (52%) activities. Finally, the WPI-EGCG conjugates remarkably improved probiotic viability (8.55 ± 0.1 log cfu/g) during 30 days of storage in an apple juice drink of pH (3.2 ± 0.01). Hence, the WPI-EGCG conjugate represents a propitious carrier to enhance probiotic functional properties upon digestion and during storage in low-pH food products.

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Section: Resultsmentioning

confidence: 94%

Enhanced In Vitro Functionality and Food Application of Lactobacillus acidophilus Encapsulated in a Whey Protein Isolate and (−)-Epigallocatechin-3-Gallate Conjugate

Bora

Lü

et al. 2021

J. Agric. Food Chem.

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“…Fluorescence quenching was calculated using the Stern–Volmer equation [ 52 ]:

where F 0 and F are the fluorescence intensities of the proteins in the absence or presence of proanthocyanidins (quencher), respectively; K sv is the Stern–Volmer quenching constant; [Q] is the concentration of quencher; K q is the bimolecular quenching constant; and τ 0 is the lifetime of the fluorophore when the quencher is absent, and the value typically equals to 10 −8 s.…”

Section: Methodsmentioning

confidence: 99%

Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage

2021

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Whey proteins and oligomeric proanthocyanidins have nutritional value and are widely used in combination as food supplements. However, the effect of the interactions between proanthocyanidins and whey proteins on their stability has not been studied in depth. In this work, we aimed to characterize the interactions between β-Lactoglobulin (β-LG) and α-lactalbumin (α-LA) and oligomeric proanthocyanidins, including A1, A2, B1, B2, B3, and C1, using multi-spectroscopic and molecular docking methods. Fluorescence spectroscopic data revealed that all of the oligomeric proanthocyanidins quenched the intrinsic fluorescence of β-LG or α-LA by binding-related fluorescence quenching. Among the six oligomeric proanthocyanidins, A1 showed the strongest affinity for β-LG (Ka = 2.951 (±0.447) × 104 L∙mol−1) and α-LA (Ka = 1.472 (±0.236) × 105 L∙mol−1) at 297 K. β-LG/α-LA and proanthocyanidins can spontaneously form complexes, which are mainly induced by hydrophobic interactions, hydrogen bonds, and van der Waals forces. Fourier-transform infrared spectroscopy (FTIR) and circular dichroism spectroscopy showed that the secondary structures of the proteins were rearranged after binding to oligomeric proanthocyanidins. During in vitro gastrointestinal digestion, the recovery rate of A1 and A2 increased with the addition of WPI by 11.90% and 38.43%, respectively. The addition of WPI (molar ratio of 1:1) increased the retention rate of proanthocyanidins A1, A2, B1, B2, B3, and C1 during storage at room temperature by 14.01%, 23.14%, 30.09%, 62.67%, 47.92%, and 60.56%, respectively. These results are helpful for the promotion of protein–proanthocyanidin complexes as functional food ingredients in the food industry.

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“…Molecular interactions might be the outcome of excited-state reactions, molecular rearrangements, energy transfer, ground-state complexation and collisional quenching [88]. Often, they result in luminance (fluorescence) quenching, which is either static or dynamic [89]. Fluorescence emission spectra are commonly utilised to determine the type of quenching with the Stern-Volmer equation [89,90],…”

Section: Overview Of the Kinetic And Thermodynamic Approach On Proteimentioning

confidence: 99%

“…Often, they result in luminance (fluorescence) quenching, which is either static or dynamic [89]. Fluorescence emission spectra are commonly utilised to determine the type of quenching with the Stern-Volmer equation [89,90],…”

Section: Overview Of the Kinetic And Thermodynamic Approach On Proteimentioning

confidence: 99%

Molecular Functionality of Plant Proteins from Low- to High-Solid Systems with Ligand and Co-Solute

Paramita¹,

Panyoyai

Kasapis

2020

IJMS

Self Cite

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In the food industry, proteins are regarded as multifunctional systems whose bioactive hetero-polymeric properties are affected by physicochemical interactions with the surrounding components in formulations. Due to their nutritional value, plant proteins are increasingly considered by the new product developer to provide three-dimensional assemblies of required structure, texture, solubility and interfacial/bulk stability with physical, chemical or enzymatic treatment. This molecular flexibility allows them to form systems for the preservation of fresh food, retention of good nutrition and interaction with a range of microconstituents. While, animal- and milk-based proteins have been widely discussed in the literature, the role of plant proteins in the development of functional foods with enhanced nutritional profile and targeted physiological effects can be further explored. This review aims to look into the molecular functionality of plant proteins in relation to the transport of bioactive ingredients and interaction with other ligands and proteins. In doing so, it will consider preparations from low- to high-solids and the effect of structural transformation via gelation, phase separation and vitrification on protein functionality as a delivery vehicle or heterologous complex. Applications for the design of novel functional foods and nutraceuticals will also be discussed.

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Combined spectroscopic, molecular docking and quantum mechanics study of β-casein and ferulic acid interactions following UHT-like treatment

Cited by 55 publications

References 39 publications

Enhanced In Vitro Functionality and Food Application of Lactobacillus acidophilus Encapsulated in a Whey Protein Isolate and (−)-Epigallocatechin-3-Gallate Conjugate

Enhanced In Vitro Functionality and Food Application of Lactobacillus acidophilus Encapsulated in a Whey Protein Isolate and (−)-Epigallocatechin-3-Gallate Conjugate

Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage

Molecular Functionality of Plant Proteins from Low- to High-Solid Systems with Ligand and Co-Solute

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