Dataset Information

Binding of β-lactoglobulin to three phenolics improves the stability of phenolics studied by multispectral analysis and molecular modeling.

ABSTRACT: Phenolics have been used to suppress the formation of advanced glycation end products (AGEs) in food; however, enhancing their thermostability and photostability in foods remains a key issue. Ferulic acid (FA), quercetin (QT), and vanillic acid (VA), which reduce production of AGEs, were embedded in bovine β-lactoglobulin (β-LG) and their interaction mechanism was investigated. Fluorescence experiments demonstrated that FA and QT displayed typical static quenching, while VA caused fluorescence sensitization of β-LG. Furthermore, phenolics changed the secondary structure of β-LG by inducing the transformation from α-helices to β-structures, with Van der Waals forces and hydrogen bonds as the primary underlying forces. The thermal and photostability of FA/QT/VA was significantly improved upon binding to β-LG. Furthermore, QT, FA and VA demonstrated good AGEs inhibitory abilities in BSA-fructose, BSA-MGO, arginine-MGO models. These results reveal that β-LG embedding effectively improves the thermostability and photostability of dietary phenolics in food.

SUBMITTER: Zhang S

PROVIDER: S-EPMC9234335 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Binding of β-lactoglobulin to three phenolics improves the stability of phenolics studied by multispectral analysis and molecular modeling.

Zhang Shanying S Li Xiaolei X Ai Binling B Zheng Lili L Zheng Xiaoyan X Yang Yang Y Xiao Dao D Sheng Zhanwu Z

Food chemistry: X 20220615

Phenolics have been used to suppress the formation of advanced glycation end products (AGEs) in food; however, enhancing their thermostability and photostability in foods remains a key issue. Ferulic acid (FA), quercetin (QT), and vanillic acid (VA), which reduce production of AGEs, were embedded in bovine β-lactoglobulin (β-LG) and their interaction mechanism was investigated. Fluorescence experiments demonstrated that FA and QT displayed typical static quenching, while VA caused fluorescence s ...[more]

PMID: 35769329

Similar Datasets

Project description:Bovine beta-lactoglobulin A assumes a dimeric native conformation at neutral pH, while the conformation at pH 2 is monomeric but still native. Beta-lactoglobulin A has a free thiol at Cys121, which is buried between the beta-barrel and the C-terminal major alpha-helix. This thiol group was specifically reacted with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) in the presence of 1.0 M Gdn-HCI at pH 7.5, producing a modified beta-lactoglobulin (TNB-bIg) containing a mixed disulfide bond with 5-thio-2-nitrobenzoic acid (TNB). The conformation and stability of TNB-bIg were studied by circular dichroism (CD), tryptophan fluorescence, analytical ultracentrifugation, and one-dimensional 1H-NMR. The CD spectra of TNB-bIg indicated disordering of the native secondary structure at pH 7.5, whereas a slight increase in the alpha-helical content was observed at pH 2.0. The tryptophan fluorescence of TNB-bIg was significantly quenched compared with that of the intact protein, probably by the energy transfer to TNB. Sedimentation equilibrium analysis indicated that, at neutral pH, TNB-bIg is monomeric while the intact protein is dimeric. In contrast, at pH 2.0, both the intact beta-lactoglobulin and TNB-bIg were monomeric. The unfolding transition of TNB-bIg induced by Gdn-HCl was cooperative in both pH regions, although the degree of cooperativity was less than that of the intact protein. The 1H-NMR spectrum for TNB-bIg at pH 3.0 was native-like, whereas the spectrum at pH 7.5 was similar to that of the unfolded proteins. These results suggest that modification of the buried thiol group destabilizes the rigid hydrophobic core and the dimer interface, producing a monomeric state that is native-like at pH 2.0 but is molten globule-like at pH 7.5. Upon reducing the mixed disulfide of TNB-bIg with dithiothreitol, the intact beta-lactoglobulin was regenerated. TNB-bIg will become a useful model to analyze the conformation and stability of the intermediate of protein folding.

Dataset Information

Binding of β-lactoglobulin to three phenolics improves the stability of phenolics studied by multispectral analysis and molecular modeling.

Publications

Binding of β-lactoglobulin to three phenolics improves the stability of phenolics studied by multispectral analysis and molecular modeling.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets