Protective effects of bovine serum albumin on blueberry anthocyanins under illumination conditions and their mechanism analysis

Lang, Yuxi; Li, Enhui; Meng, Xianjun; Tian, Jinlong; Ran, Xu-Long; Zhang, Ye; Zang, Zhihuan; Wang, Weisheng; B, Li

doi:10.1016/j.foodres.2019.05.021

Cited by 71 publications

(40 citation statements)

References 35 publications

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“…This finding is explained by an alteration in the microenvironment of the tryptophan residues in BSA, the fluorophore responsible by BSA fluorescence when excited at 295 nm. This conclusion was supported by synchronous fluorescence experiments, which is able to detect alterations in the microenvironment around tyrosine (Δ λ = 15 nm) and tryptophan residues (Δ λ = 60 nm) provoked by potential ligands . The synchronous spectra of BSA at Δ λ = 15 nm and Δ λ = 60 nm in the absence and presence of various concentrations of G8 are shown in Figure S4.…”

Section: Resultsmentioning

confidence: 60%

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Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Bertozo

Fernandes

Yoguim

et al. 2020

J of Molecular Recognition

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Fluorescence quenching is widely used to obtain association constants between proteins and ligands. This methodology is based on assumption that ground-state complex between protein and ligand is responsible for quenching. Here, we call the attention about the risk of using the temperature criterion for decision of applying or not fluorescence quenching data to measure association constants. We demonstrated that hydrophobic effect can be the major force involved in the interaction and, as such, superposes the well-established rationalization that host/guest com-

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Section: Resultsmentioning

confidence: 60%

“…The synchronous fluorescence spectra were obtained by scanning simultaneously with a fixed wavelength between the excitation and emission monochromators. The excitation wavelength was set at the range 250 to 400 nm for Δ λ of 15 nm and 220 to 350 nm for Δ λ of 60 nm . The slit width was set at 10 nm.…”

Section: Methodsmentioning

confidence: 99%

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Bertozo

Fernandes

Yoguim

et al. 2020

J of Molecular Recognition

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“…These results indicated that the interaction between anthocyanins and proteins affected the secondary structure of the complex. Lang et al (2019b) combined bovine serum albumin with blueberry anthocyanin, and found that the content of a-helix increased from 42.40% to 52.80%, the content of b-sheet decreased from 15.00% to 8.50%. Chen et al (2019) combined black soybean seed coat anthocyanin with SPI, and CD analysis showed that the a-helix content of complex decreased from 23.15% to 20.53%, the b-sheet content increased from 32.00% to 36.43%, and the b-turn and random coil contents changed only slightly.…”

Section: Structural Characterizationmentioning

confidence: 99%

“…and from 800 to 400 a.u. Lang et al (2019b) combined bovine serum albumin with blueberry anthocyanin. By fluorescence spectroscopy, the fluorescence intensities of the complex before and after adding the blueberry anthocyanin were 700 and 350 a.u., respectively.…”

Section: Review On the Interaction Between Anthocyanins And Proteins From Different Sourcesmentioning

confidence: 99%

“…By calculating, ÁG < 0 indicates the reaction was spontaneous; ÁH < 0, the reaction was an exothermic reaction; ÁS < 0, the reaction proceeded in an orderly direction; ÁH < 0 and ÁS < 0, the interactions between complex were mainly van der Waals forces and hydrogen bond. Lang et al (2019b) combined blueberry anthocyanin extracts with bovine serum albumin. The formula calculated ÁG < 0, indicating that the interaction between anthocyanins and proteins was spontaneous; ÁH > 0, the reaction was an endothermic reaction; ÁS < 0, the reaction proceeded in an orderly direction; ÁH > 0, ÁS < 0, the interaction of complex was mainly caused by electrostatic and hydrophobic forces.…”

Section: Intermolecular Interactionmentioning

confidence: 99%

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A review of the interaction between anthocyanins and proteins

Wang

et al. 2020

Food sci. technol. int.

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Anthocyanins have good physiological functions, but they are unstable. The interaction between anthocyanins and proteins can improve the stability, nutritional and functional properties of the complex. This paper reviews the structural changes of complex of anthocyanins interacting with proteins from different sources. By circular dichroism (CD) spectroscopy, it was found that the contents of α-helix (from 15.90%−42.40% to 17.60%−52.80%) or β-sheet (from 29.00%−50.00% to 29.40%−57.00%) of the anthocyanins–proteins complex increased. Fourier transform infrared spectroscopy showed that the regions of amide I (from 1627.87−1641.41 cm−1 to 1643.34−1651.02 cm−1) and amide II (from 1537.00−1540.25 cm−1 to 1539.00−1543.75 cm−1) of anthocyanins–proteins complex were shifted. Fluorescence spectroscopy showed that the fluorescence intensity of the complex decreased from 150−5100 to 40−3900 a.u. The thermodynamic analysis showed that there were hydrophobic interactions, electrostatic and hydrogen bonding interactions between anthocyanins and proteins. The kinetic analysis showed that the half-life and activation energy of the complex increased. The stability, antioxidant, digestion, absorption, and emulsification of the complex were improved. This provides a reference for the study and application of anthocyanins and proteins interactions.

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Protein and Peptide‐Based Nanotechnology for Enhancing Stability, Bioactivity, and Delivery of Anthocyanins

Zhang

Yao

Zhao

et al. 2023

Adv Healthcare Materials

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Anthocyanin, a unique natural polyphenol, is abundant in plants and widely utilized in biomedicine, cosmetics, and the food industry due to its excellent antioxidant, anticancer, antiaging, antimicrobial, and anti‐inflammatory properties. However, the degradation of anthocyanin in an extreme environment, such as alkali pH, high temperatures, and metal ions, limits its physiochemical stabilities and bioavailabilities. Encapsulation and combining anthocyanin with biomaterials could efficiently stabilize anthocyanin for protection. Promisingly, natural or artificially designed proteins and peptides with favorable stabilities, excellent biocapacity, and wide sources are potential candidates to stabilize anthocyanin. This review focuses on recent progress, strategies, and perspectives on protein and peptide for anthocyanin functionalization and delivery, i.e., formulation technologies, physicochemical stability enhancement, cellular uptake, bioavailabilities, and biological activities development. Interestingly, due to the simplicity and diversity of peptide structure, the interaction mechanisms between peptide and anthocyanin could be illustrated. This work sheds light on the mechanism of protein/peptide–anthocyanin nanoparticle construction and expands on potential applications of anthocyanin in nutrition and biomedicine.

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Protective effects of bovine serum albumin on blueberry anthocyanins under illumination conditions and their mechanism analysis

Cited by 71 publications

References 35 publications

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

A review of the interaction between anthocyanins and proteins

Protein and Peptide‐Based Nanotechnology for Enhancing Stability, Bioactivity, and Delivery of Anthocyanins

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