Complexation of whey protein with caffeic acid or (−)-epigallocatechin-3-gallate as a strategy to induce oral tolerance to whey allergenic proteins

Pessato, Tássia Batista; Carvalho, Natália C.; Figueiredo, Daniella de; Colomeu, Talita Cristina; Fernandes, Luís Gustavo Romani; Netto, Flávia Maria; Zollner, Ricardo de Lima

doi:10.1016/j.intimp.2018.12.047

Cited by 24 publications

(15 citation statements)

References 55 publications

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“…The method described by Pessato et al [ 11 ] was used for the complexation process. After mixing the proteins solutions with the CA stock solution in proportions to achieve the molar complexation ratios of 1:1 and 1:2 (protein concentration fixed at 5 mg/mL), the complexation was carried out at 25 °C for 60 min in the dark, using 0.1 M HCl to adjust the pH to 3.5.…”

Section: Methodsmentioning

confidence: 99%

“…The biological activity of CA was demonstrated in vitro and in vivo, as providing innumerable physiological effects, such as antibacterial activity [ 1 ], antiviral activity [ 2 ], antioxidant activity [ 3 ], anti-inflammatory activity [ 4 ], anti-atherosclerotic activity [ 5 ], immunostimulatory activity [ 6 ], antidiabetic activity [ 3 ], cardioprotective activity [ 7 ], antiproliferative activity [ 8 ], hepatoprotective activity [ 9 ], anticancer activity [ 2 , 3 ], and anti-hepatocellular carcinoma activity [ 10 ]. Additionally, Pessato et al [ 11 ] showed that the complexation of whey protein isolate (WPI) with CA was able to attenuate oral sensitization in C3H/HeJ mice against WPI.…”

Section: Introductionmentioning

confidence: 99%

“…However, many studies carried out on conformational β-LG changes contribute to changes in the emerging allergenicity [ 20 ]. It has been demonstrated that the binding of different ligands to β-LG changes their biological activity [ 11 , 21 ].…”

Section: Introductionmentioning

confidence: 99%

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The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes

et al. 2020

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In this study, the interaction of native and transglutaminase (Tgase) cross-linked β-lactoglobulin (β-LG) with caffeic acid (CA) was examined, aiming to obtain functional composites. Knowledge on the binding affinity and interaction mechanism was provided by performing fluorescence spectroscopy measurements, after heating the native and cross-linked protein at temperatures ranging from 25 to 95 °C. Regardless of the protein aggregation state, a static quenching mechanism of intrinsic fluorescence of β-LG by CA was established. The decrease of the Stern–Volmer constants with the temperature increase indicating the facile dissociation of the weakly bound complexes. The thermodynamic analysis suggested the existence of multiple contact types, such as Van der Waals’ force and hydrogen bonds, between β-LG and CA. Further molecular docking tests indicated the existence of various CA binding sites on the β-LG surface heat-treated at different temperatures. Anyway, regardless of the simulated temperature, the CA-β-LG assemblies appeared to be unstable. Compared to native protein, the CA-β-LG and CA-β-LGTgase complexes (ratio 1:1) exhibited significantly higher antioxidant activity and inhibitory effects on α-glucosidase, α-amylase, and pancreatic lipase, enzymes associated with metabolic syndrome. These findings might help the knowledge-based development of novel food ingredients with valuable biological properties.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes

et al. 2020

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“…These processes change the structure of WPs via biological activity alteration, so their health properties are changed, as there are numerous physicochemical modifications that need to be investigated to overcome these flaws and increase the functions of WPs (Madhan et al 2005;Cao et al 2018;Rasouli et al 2019). The techno-functional properties of WPs are improved by their linking to food-grade products and are bonded to polysaccharides and polyphenols via covalent linkages or noncovalent linkages (Cao et al 2018;Setiowati et al 2020) and thereby improve the techno-functional qualities of the protein with the biological qualities (Doost et al 2019;Khalifa et al 2019;Pessato et al 2019;Wang et al 2020a,b;Zhong et al 2021). Recently, there have been advancements in modified protein manufacturing that resulted in enhanced biological and techno-functional properties, with rapid advances in food science technology applications (Chen et al 2021).…”

Section: Whey Protein-polyphenol Conjugates and Complexesmentioning

confidence: 99%

A review of polyphenol and whey protein-based conjugates

Tazeddinova

Toshev

Абылгазинова

et al. 2022

BioRes

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Proteins act as a primary food component obtained from different food sources. In contrast, polyphenols are metabolites and are abundantly present in plants, so their combination plays a crucial role in defining the functional properties of a food product. In the current review, the protein-polyphenol interactions have been briefly reviewed, along with the changes that occur because of their interaction. The mechanisms and the factors affecting the functionalities of the protein-polyphenol conjugates, e.g., the solubility, antioxidant, and gelling properties, have also been briefly reviewed. In addition, the interaction of polyphenols with whey proteins was been reviewed with various applications within the food industry, e.g., emulsifiers, foaming agents, and antioxidants. To end the review, future challenges were also highlighted.

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“…Термокальциевое осаждение основано на образовании агрегатов липидонерастворимых фосфатов кальция при умеренных температурах (50°C), нейтральном pH (7,(3)(4)(5)(6)(7)5) и присутствии кальция. Белки связаны с вышеупомянутыми фосфатными агрегатами [23,24].…”

Section: методы и процессы обработки молочной сывороткиunclassified

Whey: State of the Art. Part II. Processes and Treatment Methods

Paladii¹,

Vrabie²,

Sprincean³

et al. 2021

EOM

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The current state of the art on studying of whey is considered. The processes and methods of whey processing (thermal, chemical, physicochemical, biotechnological, and electrophysical) are presented. Thermal and isoelectric precipitation of proteins, using reagents and coagulants, as well as the main membrane processing methods (reverse osmosis, diafiltration, microfiltration, ultrafiltration, and nanofiltration) are described. Possibi-lities of effective separation of whey proteins by a combination of membrane and other methods are noted. Chromatographic methods for fractionation of whey proteins (chromatography with imitation of a moving bed, high-gradient chromatography with a magnetic trap, selective adsorption, displacement chromatography, membrane adsorption), which provide a high degree of separation, are described. Highly porous chromatographic materials providing a high flow rate, biotechnological processing methods – biosynthesis of lactulose, enzymatic hydrolysis of lactose and whey proteins, aerobic and anaerobic fermentation are considered. Electrophysical methods of processing whey (electrodialysis, electroactivation), which include electrodialysis and electro-activation, as well as electrochemical activation as a phenomenon and technology, as a new promising processing method that allows to create a waste-free cycle for obtaining valuable components and useful derivatives from whey without the use of reagents are analyzed. It is emphasized that, depending on the regimes used, protein-mineral concentrates with a predetermined protein or mineral composition are obtained with the simultaneous isomerization of lactose into lactulose. It is stated that the efficiency of methods for processing whey is ensured by a significant increase in the efficiency of technological processes, a decrease in labor costs, a reduction in the processing time and materials, and an improvement in the quality and functional properties of the final products.

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Complexation of whey protein with caffeic acid or (−)-epigallocatechin-3-gallate as a strategy to induce oral tolerance to whey allergenic proteins

Cited by 24 publications

References 55 publications

The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes

The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes

A review of polyphenol and whey protein-based conjugates

Whey: State of the Art. Part II. Processes and Treatment Methods

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