Evaluation of the dilational modulus of protein films by pendant bubble tensiometry

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Evaluation of the dilational modulus of protein films by pendant bubble tensiometry. / Tseng, Wen Chi; Tsay, Ruey Yug; Le, Thu Thi Yen; Hussain, Siam; Noskov, Boris A.; Akentiev, Alexander; Yeh, Hsu Hsiang; Lin, Shi Yow.

в: Journal of Molecular Liquids, Том 349, 118113, 01.03.2022.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Author

Tseng, Wen Chi ; Tsay, Ruey Yug ; Le, Thu Thi Yen ; Hussain, Siam ; Noskov, Boris A. ; Akentiev, Alexander ; Yeh, Hsu Hsiang ; Lin, Shi Yow. / Evaluation of the dilational modulus of protein films by pendant bubble tensiometry. в: Journal of Molecular Liquids. 2022 ; Том 349.

BibTeX

@article{4bb02fde02cd461db5ce5c610798198f,

title = "Evaluation of the dilational modulus of protein films by pendant bubble tensiometry",

abstract = "A new approach for evaluating the dilational modulus of an adsorbed protein film was proposed in this study; wherein, the air-water interface of Bovine serum albumin (BSA) aqueous solution was not subjected to a forced perturbation. The approach involved: (i) monitoring the relaxations of surface tension (ST), surface area (SA), and ambient/solution temperature of aqueous bovine serum albumin (BSA) solution using a pendant bubble tensiometer and (ii) detecting the numerous minute and low-frequency interfacial perturbances in the SA and ST relaxations (resultant from the minute variations in ambient temperature) at the latter stages of BSA adsorption process. For these perturbances, their surface dilational rate (dlnA/dt) and rate of ST change (dγ/dt) were determined, and then the dilational modulus (E = dγ/dlnA) was obtained from the slope of the linear best-fit in the plot of dγ/dt vs dlnA/dt. Using this approach, the dilational modulus of the adsorbed BSA film at a concentration of 0.052 and 15 (10−10 mol/cm3) was found to be 43 and 30 mN/m, respectively.",

keywords = "Bovine serum albumin, Dilational modulus, Pendant bubble tensiometry, Protein film, Surface tension relaxation",

author = "Tseng, {Wen Chi} and Tsay, {Ruey Yug} and Le, {Thu Thi Yen} and Siam Hussain and Noskov, {Boris A.} and Alexander Akentiev and Yeh, {Hsu Hsiang} and Lin, {Shi Yow}",

note = "Publisher Copyright: {\textcopyright} 2021 Elsevier B.V.",

year = "2022",

month = mar,

day = "1",

doi = "10.1016/j.molliq.2021.118113",

language = "English",

volume = "349",

journal = "Journal of Molecular Liquids",

issn = "0167-7322",

publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Evaluation of the dilational modulus of protein films by pendant bubble tensiometry

AU - Tseng, Wen Chi

AU - Tsay, Ruey Yug

AU - Le, Thu Thi Yen

AU - Hussain, Siam

AU - Noskov, Boris A.

AU - Akentiev, Alexander

AU - Yeh, Hsu Hsiang

AU - Lin, Shi Yow

PY - 2022/3/1

Y1 - 2022/3/1

N2 - A new approach for evaluating the dilational modulus of an adsorbed protein film was proposed in this study; wherein, the air-water interface of Bovine serum albumin (BSA) aqueous solution was not subjected to a forced perturbation. The approach involved: (i) monitoring the relaxations of surface tension (ST), surface area (SA), and ambient/solution temperature of aqueous bovine serum albumin (BSA) solution using a pendant bubble tensiometer and (ii) detecting the numerous minute and low-frequency interfacial perturbances in the SA and ST relaxations (resultant from the minute variations in ambient temperature) at the latter stages of BSA adsorption process. For these perturbances, their surface dilational rate (dlnA/dt) and rate of ST change (dγ/dt) were determined, and then the dilational modulus (E = dγ/dlnA) was obtained from the slope of the linear best-fit in the plot of dγ/dt vs dlnA/dt. Using this approach, the dilational modulus of the adsorbed BSA film at a concentration of 0.052 and 15 (10−10 mol/cm3) was found to be 43 and 30 mN/m, respectively.

AB - A new approach for evaluating the dilational modulus of an adsorbed protein film was proposed in this study; wherein, the air-water interface of Bovine serum albumin (BSA) aqueous solution was not subjected to a forced perturbation. The approach involved: (i) monitoring the relaxations of surface tension (ST), surface area (SA), and ambient/solution temperature of aqueous bovine serum albumin (BSA) solution using a pendant bubble tensiometer and (ii) detecting the numerous minute and low-frequency interfacial perturbances in the SA and ST relaxations (resultant from the minute variations in ambient temperature) at the latter stages of BSA adsorption process. For these perturbances, their surface dilational rate (dlnA/dt) and rate of ST change (dγ/dt) were determined, and then the dilational modulus (E = dγ/dlnA) was obtained from the slope of the linear best-fit in the plot of dγ/dt vs dlnA/dt. Using this approach, the dilational modulus of the adsorbed BSA film at a concentration of 0.052 and 15 (10−10 mol/cm3) was found to be 43 and 30 mN/m, respectively.

KW - Bovine serum albumin

KW - Dilational modulus

KW - Pendant bubble tensiometry

KW - Protein film

KW - Surface tension relaxation

UR - http://www.scopus.com/inward/record.url?scp=85119897473&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/741eb09a-0110-3f87-a4dc-cbcc25bd9f45/

U2 - 10.1016/j.molliq.2021.118113

DO - 10.1016/j.molliq.2021.118113

M3 - Article

AN - SCOPUS:85119897473

VL - 349

JO - Journal of Molecular Liquids

JF - Journal of Molecular Liquids

SN - 0167-7322

M1 - 118113

ER -

ID: 89536266

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