Interactions and emulsifying properties of ovalbumin with tannic acid

Yang, Czau‐Siung; Hu, Jie; Yi, Xiangzhou; Ding, Baomiao; Sun, Weiqing; Yan, Fei; Wei, Shudong; Li, Zhenshun

doi:10.1016/j.lwt.2018.04.088

Cited by 89 publications

(23 citation statements)

References 47 publications

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“…Finally, because TA has the property of binding to proteins in a non-specific manner, it is also likely that the binding of the antigenic protein and TA may physically prevent the capture of immune cells. This is supported by the findings of Chen et al, which show that TA binds strongly to OVAs [ 27 , 28 , 29 ].…”

Section: Discussionsupporting

confidence: 78%

Co-Application with Tannic Acid Prevents Transdermal Sensitization to Ovalbumin in Mice

Izumi

Tanahashi

Kinugasa

et al. 2022

IJMS

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Transdermal sensitization to allergens is of great concern as a sensitization route for food allergies. This skin-mediated invasion and sensitization to allergens is involved in skin barrier breakdown and inflammation, followed by the production of several kinds of cytokines. Cytokines such as thymic stromal lymphopoietin and thymus and activation-regulated chemokine are also involved. In this study, we investigated the suppressive effect of tannic acid (TA) on transdermal sensitization using ovalbumin (OVA), a major egg-white allergen. We also analyzed the mechanisms associated with the inhibitory effects of TA. The results showed that the co-application with TA prevents transdermal sensitization to OVA. As possible mechanisms, its anti-inflammatory and astringent effect on the skin and binding ability with the protein were considered. These results indicate that TA could be applied to cosmetics and lotions, which could suppress the transdermal sensitization to allergens.

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Section: Discussionsupporting

confidence: 78%

Co-Application with Tannic Acid Prevents Transdermal Sensitization to Ovalbumin in Mice

Izumi

Tanahashi

Kinugasa

et al. 2022

IJMS

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“…The total biopolymer concentration was 0.1% (w/w). The native OVA solution had an isoelectric point (IEP) of 4.70 which was corresponding to the literature value 4.75 (Chen et al, 2018). The strongest reduction of IEP was observed for the OVA-inulin incubated for 10 days, which was down to around 4.10.…”

Section: Characterization Of Ova Glycated By Inulinsupporting

confidence: 76%

Pomegranate seed oil stabilized with ovalbumin glycated by inulin: Physicochemical stability and oxidative stability

Wang

Han

et al. 2020

Food Hydrocolloids

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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“…On the other hand, the interaction also affected the conformation, functional and nutritional properties of OVA 5 . Studies indicated that the combination of OVA and tannic acid reduced the surface activity, thus decreasing the emulsifying ability of proteins 17 . Caffeic acid enhanced the foaming property of OVA via increasing the content of OVAʼs flexible structure 18 .…”

Section: Introductionmentioning

confidence: 99%

Exploring the binding mechanism of ferulic acid and ovalbumin: insights from spectroscopy, molecular docking and dynamics simulation

Chen

Zhu

et al. 2022

J Sci Food Agric

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BACKGROUND: Ferulic acid (FA), a phenolic acid widely occurring in nature, has attracted extensive attention because of its biological activity. Ovalbumin (OVA) is a commonly used carrier protein. The mechanism of FA binding with OVA was investigated by utilizing a variety of spectral analyses, accompanied by computer simulation. RESULTS: It was discovered that the fluorescence quenching mechanism of OVA by FA was a static mode as a result of the formation of an FA−OVA complex, which was verified by the concentration distributions and pure spectrum of the constituents decomposed from the high overlap spectrum signals using multivariate curve resolution-alternate least squares algorithm. Hydrogen bonds and Van der Waals forces drove the formation of FA-OVA complex with a binding constant of 1.69 × 10 4 L mol −1 . The presence of FA induced the loose structure of OVA with an attenuation of ⊍-helix content and improved the thermal stability of OVA. Computer docking indicated that FA interacted with the amino acid residues Arg84, Asn88, Leu101 and Ser103 of OVA through hydrogen bonds. Molecular dynamics simulation proved that the combination of FA with OVA boosted the conformational stability of OVA and hydrogen bonds brought a crucial part in stabilizing the structure of the complex. CONCLUSIONS:The study may supply the theoretical basis for the design of FA transport system using OVA as carrier protein to improve the instability and low bioavailability of FA.

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Interactions and emulsifying properties of ovalbumin with tannic acid

Cited by 89 publications

References 47 publications

Co-Application with Tannic Acid Prevents Transdermal Sensitization to Ovalbumin in Mice

Co-Application with Tannic Acid Prevents Transdermal Sensitization to Ovalbumin in Mice

Pomegranate seed oil stabilized with ovalbumin glycated by inulin: Physicochemical stability and oxidative stability

Exploring the binding mechanism of ferulic acid and ovalbumin: insights from spectroscopy, molecular docking and dynamics simulation

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