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On the equilibrium surface tension of aqueous protein solutions – Bovine serum albumin. / Thi-Yen Le, Thu; Hussain, Siam; Tsay, Ruey Yug; Noskov, Boris A.; Akentiev, Alexander; Lin, Shi Yow.

In: Journal of Molecular Liquids, Vol. 347, 118305, 01.02.2022.

Research output: Contribution to journal › Article › peer-review

Harvard

Thi-Yen Le, T, Hussain, S, Tsay, RY, Noskov, BA, Akentiev, A & Lin, SY 2022, 'On the equilibrium surface tension of aqueous protein solutions – Bovine serum albumin', Journal of Molecular Liquids, vol. 347, 118305. https://doi.org/10.1016/j.molliq.2021.118305

APA

Thi-Yen Le, T., Hussain, S., Tsay, R. Y., Noskov, B. A., Akentiev, A., & Lin, S. Y. (2022). On the equilibrium surface tension of aqueous protein solutions – Bovine serum albumin. Journal of Molecular Liquids, 347, [118305]. https://doi.org/10.1016/j.molliq.2021.118305

Vancouver

Thi-Yen Le T, Hussain S, Tsay RY, Noskov BA, Akentiev A, Lin SY. On the equilibrium surface tension of aqueous protein solutions – Bovine serum albumin. Journal of Molecular Liquids. 2022 Feb 1;347. 118305. https://doi.org/10.1016/j.molliq.2021.118305

Author

Thi-Yen Le, Thu ; Hussain, Siam ; Tsay, Ruey Yug ; Noskov, Boris A. ; Akentiev, Alexander ; Lin, Shi Yow. / On the equilibrium surface tension of aqueous protein solutions – Bovine serum albumin. In: Journal of Molecular Liquids. 2022 ; Vol. 347.

BibTeX

@article{5ed1b44018994648a5f7b5a27c9b26c7,
title = "On the equilibrium surface tension of aqueous protein solutions – Bovine serum albumin",
abstract = "The dynamic and equilibrium surface tension (ST) data of proteins such as bovine serum albumin (BSA) are crucial in numerous theoretical and practical applications. However, reliable equilibrium ST of BSA is absent in the literature. This study illustrates a more precise and accurate approach for measuring equilibrium ST of aqueous BSA solutions. The ST relaxation of aqueous BSA solution [C = 0.052–15 (10-10 mol/cm3)] was monitored using a pendant bubble tensiometer for 2–5 days, depending on the BSA concentration. The dynamic ST indicated that irrespective of the BSA concentration, the ST remained nearly constant at the latter stage for several tens of hours. These ST values were further confirmed by a perturbation process (a forced, rapid expansion/compression of the bubble surface). The data indicated that the equilibrium ST of BSA(aq) solutions remained essentially unchanged over a wide range of BSA concentration [C = 0.052 to 15 (10-10 mol/cm3)] at 51.5 ± 0.3 mN/m.",
keywords = "Bovine serum albumin, Dynamic surface tension, Equilibrium surface tension, Pendant bubble tensiometry, Perturbed interface, Protein, AIR/WATER INTERFACE, FILM, LACTOGLOBULIN, BETA-CASEIN ADSORPTION, AIR-WATER, KINETICS, ALPHA-LACTALBUMIN, PLATE",
author = "{Thi-Yen Le}, Thu and Siam Hussain and Tsay, {Ruey Yug} and Noskov, {Boris A.} and Alexander Akentiev and Lin, {Shi Yow}",
note = "Publisher Copyright: {\textcopyright} 2021 Elsevier B.V.",
year = "2022",
month = feb,
day = "1",
doi = "10.1016/j.molliq.2021.118305",
language = "English",
volume = "347",
journal = "Journal of Molecular Liquids",
issn = "0167-7322",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - On the equilibrium surface tension of aqueous protein solutions – Bovine serum albumin

AU - Thi-Yen Le, Thu

AU - Hussain, Siam

AU - Tsay, Ruey Yug

AU - Noskov, Boris A.

AU - Akentiev, Alexander

AU - Lin, Shi Yow

N1 - Publisher Copyright: © 2021 Elsevier B.V.

PY - 2022/2/1

Y1 - 2022/2/1

N2 - The dynamic and equilibrium surface tension (ST) data of proteins such as bovine serum albumin (BSA) are crucial in numerous theoretical and practical applications. However, reliable equilibrium ST of BSA is absent in the literature. This study illustrates a more precise and accurate approach for measuring equilibrium ST of aqueous BSA solutions. The ST relaxation of aqueous BSA solution [C = 0.052–15 (10-10 mol/cm3)] was monitored using a pendant bubble tensiometer for 2–5 days, depending on the BSA concentration. The dynamic ST indicated that irrespective of the BSA concentration, the ST remained nearly constant at the latter stage for several tens of hours. These ST values were further confirmed by a perturbation process (a forced, rapid expansion/compression of the bubble surface). The data indicated that the equilibrium ST of BSA(aq) solutions remained essentially unchanged over a wide range of BSA concentration [C = 0.052 to 15 (10-10 mol/cm3)] at 51.5 ± 0.3 mN/m.

AB - The dynamic and equilibrium surface tension (ST) data of proteins such as bovine serum albumin (BSA) are crucial in numerous theoretical and practical applications. However, reliable equilibrium ST of BSA is absent in the literature. This study illustrates a more precise and accurate approach for measuring equilibrium ST of aqueous BSA solutions. The ST relaxation of aqueous BSA solution [C = 0.052–15 (10-10 mol/cm3)] was monitored using a pendant bubble tensiometer for 2–5 days, depending on the BSA concentration. The dynamic ST indicated that irrespective of the BSA concentration, the ST remained nearly constant at the latter stage for several tens of hours. These ST values were further confirmed by a perturbation process (a forced, rapid expansion/compression of the bubble surface). The data indicated that the equilibrium ST of BSA(aq) solutions remained essentially unchanged over a wide range of BSA concentration [C = 0.052 to 15 (10-10 mol/cm3)] at 51.5 ± 0.3 mN/m.

KW - Bovine serum albumin

KW - Dynamic surface tension

KW - Equilibrium surface tension

KW - Pendant bubble tensiometry

KW - Perturbed interface

KW - Protein

KW - AIR/WATER INTERFACE

KW - FILM

KW - LACTOGLOBULIN

KW - BETA-CASEIN ADSORPTION

KW - AIR-WATER

KW - KINETICS

KW - ALPHA-LACTALBUMIN

KW - PLATE

UR - http://www.scopus.com/inward/record.url?scp=85121282016&partnerID=8YFLogxK

U2 - 10.1016/j.molliq.2021.118305

DO - 10.1016/j.molliq.2021.118305

M3 - Article

AN - SCOPUS:85121282016

VL - 347

JO - Journal of Molecular Liquids

JF - Journal of Molecular Liquids

SN - 0167-7322

M1 - 118305

ER -

ID: 93802915