2019
DOI: 10.1039/c9nj00115h
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Gallic acid influence on bovine serum albumin thermal stability

Abstract: A thermoanalytical approach reveals the dual action of GA on BSA thermal stability.

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Cited by 32 publications
(13 citation statements)
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“…The main absorption band in each absorption spectrum of the Ag nanoparticles that is characteristic of nanosilver is visible in the wavelength range of λ = 400–500 nm 7. Additionally, other bands with peak maxima located at approximately λ = 350 nm can be noticed.…”
Section: Resultsmentioning
confidence: 92%
See 1 more Smart Citation
“…The main absorption band in each absorption spectrum of the Ag nanoparticles that is characteristic of nanosilver is visible in the wavelength range of λ = 400–500 nm 7. Additionally, other bands with peak maxima located at approximately λ = 350 nm can be noticed.…”
Section: Resultsmentioning
confidence: 92%
“…This may be due to different nanosilver concentrations in the tested products. And this may be due to the fact that gallic acid is a molecule that starts to destabilize and decompose at 68°C [7]. Additional information is given in Sect.…”
Section: High-pressure Reactormentioning
confidence: 99%
“…Specifically, dominated by the thermal diffusion of molecules and ions, the magnitude of F D and F TE increases with the temperature gradients. , Meanwhile, F E can also be controlled by the temperature field since the surface charge of BSA is sensitive to temperature. As illustrated by the grayscale image of the substrate in Figure a­(i), the hot region of the BSA-coated substrate possesses a higher surface zeta potential because the primary structure of BSA with negative charges is exposed to the solution , (Figure a­(iii-iv)). The measured zeta potentials and surface zeta potentials at different temperatures can be found in Supplementary Note 1.…”
Section: Resultsmentioning
confidence: 99%
“…The mechanism of protein denaturation inhibition of the flower extract might be due to the interaction of polyphenolic compounds in the extract and albumin protein, resulting in improved thermal stability of proteins. Binding of gallic acid with protein increased protein intramolecular packing and induced higher thermal stability [ 39 ]. Coumarin and its derivatives exhibited an inhibition of heat-induced protein denaturation at specific concentrations [ 40 , 41 ].…”
Section: Resultsmentioning
confidence: 99%