Interactions of tetracyclines with ovalbumin, the main allergen protein from egg white: Spectroscopic and electrophoretic studies

Dantas, Maria Dayanne de A.; Tenório, Humberto de Araújo; Lopes, Thiago Beirigo; Pereira, Hugo Juarez Vieira; Marsaioli, Anita Jocelyne; Figueiredo, Isis M.; Santos, Josué Carinhanha Caldas

doi:10.1016/j.ijbiomac.2017.04.052

Cited by 60 publications

(31 citation statements)

References 39 publications

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“…Ovalbumin (OVA) is the predominant protein in egg white, which is a major allergen in egg white, causing allergic reactions particularly in infants and young children. , A number of studies have investigated the use of food-processing methods for reducing OVA allergenicity, such as hydrolysis, heating, and high-pressure treatments. However, a major impediment to reduce OVA allergenicity is the risk to alter the functional attributes of OVA .…”

Section: Introductionmentioning

confidence: 99%

Effect of Covalent Interaction with Chlorogenic Acid on the Allergenic Capacity of Ovalbumin

et al. 2018

J. Agric. Food Chem.

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Ovalbumin (OVA) is a major allergen in avian egg white. Here, we investigated the conjugation of OVA and chlorogenic acid (CHA) to reduce the allergenic capacity of OVA. OVA-CHA conjugate was characterized by SDS-PAGE, MALDI-TOF-MS, differential scanning calorimetry, and multispectroscopic methods. Sites of the OVA-CHA conjugate were identified by LC-MS/MS. CHA possibly conjugated with Lys20 and Lys17 in OVA, which resulted in the unfolding of OVA. ELISA and Western blot assay indicated that the OVA-CHA conjugate reduced the IgE binding capacity of OVA. The results also indicated that the ability of the OVA-CHA conjugate to activate histamine release was reduced. The decreased allergenic capacity of OVA was attributed to changes in the protein structure. Moreover, the CHA binding site in OVA might directly shield the linear IgE epitope, thereby reducing the IgE binding ability. Also, the OVA-CHA conjugate showed high antioxidant activity. OVA conjugated with CHA may be a promising method of OVA hyposensitization.

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Section: Introductionmentioning

confidence: 99%

Effect of Covalent Interaction with Chlorogenic Acid on the Allergenic Capacity of Ovalbumin

et al. 2018

J. Agric. Food Chem.

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“…These spectral changes are best observed from the absorbance values of the 16 -ctDNA mixture (A complex = 0.8626), and the sum of the absorbance values of the free compound and ctDNA (A 16 + A ctDNA = 0.5407). Through the equation ΔA = A complex − (A compound + A ctDNA ), it is verified that the value of ΔA ≠ 0 (ΔA = 0.3219), which indicates that changes occurred in the fundamental state, characterizing a preferential mechanism of static quenching due to formation of a macromolecule-ligand complex [50] , reinforcing the results by molecular fluorescence. However, if dynamic quenching was the predominant mechanism in the interaction process, one would not expect changes, since this affects only the excited state [22] , [51] .…”

Section: Resultsmentioning

confidence: 74%

Highly functionalized piperidines: Free radical scavenging, anticancer activity, DNA interaction and correlation with biological activity

Das

Silva

et al. 2018

Journal of Advanced Research

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“…Formation of OVA-CMC complexes at pH 4.7. Since the isoelectric point of OVA is around pH 4.7 13 , the PDI values of OVA (0.753 ± 0.032) and OVA-CMC (0.583 ± 0.015) solutions were all above 0.5, indicating a poor dispersity with large size dimensions and heterogeneous distribution. OVA molecules tended to aggregate due to lack of surface charges.…”

Section: Resultsmentioning

confidence: 99%

Improving emulsion stability based on ovalbumin-carboxymethyl cellulose complexes with thermal treatment near ovalbumin isoelectric point

Kuang

Jiang

et al. 2020

Sci Rep

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Ovalbumin (OVA) is an important protein emulsifier. However, it is unstable near the isoelectric point pH, which limits its applications in the food industry. Polysaccharides may be explored to tackle this challenge by improving its pH-dependent instability. In this work, carboxymethyl cellulose (CMC) was used as a model polysaccharide to mix with OVA near its isoelectric point (pH 4.7) with subsequent mild heating at 60 °C for 30 min. The molecular interactions between OVA and CMC were comprehensively studied via a series of characterizations, including turbidity, zeta potential, intrinsic fluorescence, surface hydrophobicity, circular dichroism (CD) spectra and Fourier transform infrared spectroscopy (FTIR). The droplet sizes of the emulsions prepared by OVA-CMC were measured to analyze emulsifying property and stability. The results indicated that free OVA was easily aggregated due to loss of surface charges, while complexing with CMC significantly inhibited OVA aggregation before and after heating owing to the strong electrostatic repulsion. In addition, OVA exposed more hydrophobic clusters after heating, which resulted in the growth of surface hydrophobicity. Altogether, the heated OVA-CMC complexes presented the best emulsifying property and stability. Our study demonstrated that complexing OVA with CMC not only greatly improved its physicochemical properties but also significantly enhanced its functionality as a food-grade emulsifying agent, expanding its applications in the food industry, as development of emulsion-based acidic food products.Egg ovalbumin (OVA), the main ingredient of egg white protein, is one of the most widely used protein and a kind of important food ingredient. In addition, OVA also possesses important functionalities including emulsifying and foaming stability because it has more than 50% hydrophobic amino acids, similar to other surface-active agents 1,2 . Nevertheless, there are two major limitations for OVA to be widely used in the food industry. First, OVA is known to have poor thermal instability. It was reported that the thermal aggregation temperature of OVA was lower around its isoelectric point than that in other pH conditions, and the optimal thermal stability was in the pH range from 6 to 10 3,4 . In addition, the emulsifying property of OVA was poor near the isoelectric point as shown in our previous work 2 . Meanwhile, as a protein molecule, when the pH is reduced to around its isoelectric point (pH 4.7), OVA carries zero net surface charge and loses its emulsifying capability when used in the emulsion-based acidic food products, such as yogurt and lactic acid beverages 5 .Carboxymethyl cellulose (CMC), one of the derivatives of cellulose, has been widely used as a stabilizing agent in foods 6 . In addition, CMC is stable with strong negative charges at pH values from 2 to 10, which makes it suitable for various applications in most food products across a wide range of pH conditions. CMC is a commonly used additive to improve the processing properties of products in cos...

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Interactions of tetracyclines with ovalbumin, the main allergen protein from egg white: Spectroscopic and electrophoretic studies

Cited by 60 publications

References 39 publications

Effect of Covalent Interaction with Chlorogenic Acid on the Allergenic Capacity of Ovalbumin

Effect of Covalent Interaction with Chlorogenic Acid on the Allergenic Capacity of Ovalbumin

Highly functionalized piperidines: Free radical scavenging, anticancer activity, DNA interaction and correlation with biological activity

Improving emulsion stability based on ovalbumin-carboxymethyl cellulose complexes with thermal treatment near ovalbumin isoelectric point

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