Unique properties of bubbles and foam films stabilized by HFBII hydrophobin

Research output: Contribution to journalArticlepeer-review

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Unique properties of bubbles and foam films stabilized by HFBII hydrophobin. / Basheva, Elka S.; Kralchevsky, Peter A.; Christov, Nikolay C.; Danov, Krassimir D.; Stoyanov, Simeon D.; Blijdenstein, Theodorus B J; Kim, Hyun Jung; Pelan, Eddie G.; Lips, Alex.

In: Langmuir, Vol. 27, No. 6, 15.03.2011, p. 2382-2392.

Research output: Contribution to journalArticlepeer-review

Harvard

Basheva, ES, Kralchevsky, PA, Christov, NC, Danov, KD, Stoyanov, SD, Blijdenstein, TBJ, Kim, HJ, Pelan, EG & Lips, A 2011, 'Unique properties of bubbles and foam films stabilized by HFBII hydrophobin', Langmuir, vol. 27, no. 6, pp. 2382-2392. https://doi.org/10.1021/la104726w

APA

Basheva, E. S., Kralchevsky, P. A., Christov, N. C., Danov, K. D., Stoyanov, S. D., Blijdenstein, T. B. J., Kim, H. J., Pelan, E. G., & Lips, A. (2011). Unique properties of bubbles and foam films stabilized by HFBII hydrophobin. Langmuir, 27(6), 2382-2392. https://doi.org/10.1021/la104726w

Vancouver

Basheva ES, Kralchevsky PA, Christov NC, Danov KD, Stoyanov SD, Blijdenstein TBJ et al. Unique properties of bubbles and foam films stabilized by HFBII hydrophobin. Langmuir. 2011 Mar 15;27(6):2382-2392. https://doi.org/10.1021/la104726w

Author

Basheva, Elka S. ; Kralchevsky, Peter A. ; Christov, Nikolay C. ; Danov, Krassimir D. ; Stoyanov, Simeon D. ; Blijdenstein, Theodorus B J ; Kim, Hyun Jung ; Pelan, Eddie G. ; Lips, Alex. / Unique properties of bubbles and foam films stabilized by HFBII hydrophobin. In: Langmuir. 2011 ; Vol. 27, No. 6. pp. 2382-2392.

Bibtex

@article{f09758fc859b46cd8fbc1c5f6e232be3,
title = "Unique properties of bubbles and foam films stabilized by HFBII hydrophobin",
abstract = "The HFBII hydrophobin is an amphiphilic protein that can irreversibly adsorb at the air/water interface. The formed protein monolayers can reach a state of two-dimensional elastic solid that exhibits a high mechanical strength as compared to adsorption layers of typical amphiphilic proteins. Bubbles formed in HFBII solutions preserve the nonspherical shape they had at the moment of solidification of their surfaces. The stirring of HFBII solutions leads to the formation of many bubbles of micrometer size. Measuring the electrophoretic mobility of such bubbles, the Χ-potential was determined. Upon compression, the HFBII monolayers form periodic wrinkles of wavelength 11.5 μm, which corresponds to bending elasticity kc = 1.1 × 10-19 J. The wrinkled hydrophobin monolayers are close to a tension-free state, which prevents the Ostwald ripening and provides bubble longevity in HFBII stabilized foams. Films formed between two bubbles are studied by experiments in a capillary cell. In the absence of added electrolyte, the films are electrostatically stabilized. The appearance of protein aggregates is enhanced with the increase of the HFBII and electrolyte concentrations and at pH close to the isoelectric point. When the aggregate concentration is not too high (to block the film thinning), the films reach a state with 12 nm uniform thickness, which corresponds to two surface monolayers plus HFBII tetramers sandwiched between them. In water, the HFBII molecules can stick to each other not only by their hydrophobic moieties but also by their hydrophilic parts. The latter leads to the attachment of HFBII aggregates such as dimers, tetramers, and bigger ones to the interfacial adsorption monolayers, which provides additional stabilization of the liquid films.",
author = "Basheva, {Elka S.} and Kralchevsky, {Peter A.} and Christov, {Nikolay C.} and Danov, {Krassimir D.} and Stoyanov, {Simeon D.} and Blijdenstein, {Theodorus B J} and Kim, {Hyun Jung} and Pelan, {Eddie G.} and Alex Lips",
year = "2011",
month = mar,
day = "15",
doi = "10.1021/la104726w",
language = "English",
volume = "27",
pages = "2382--2392",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "6",

}

RIS

TY - JOUR

T1 - Unique properties of bubbles and foam films stabilized by HFBII hydrophobin

AU - Basheva, Elka S.

AU - Kralchevsky, Peter A.

AU - Christov, Nikolay C.

AU - Danov, Krassimir D.

AU - Stoyanov, Simeon D.

AU - Blijdenstein, Theodorus B J

AU - Kim, Hyun Jung

AU - Pelan, Eddie G.

AU - Lips, Alex

PY - 2011/3/15

Y1 - 2011/3/15

N2 - The HFBII hydrophobin is an amphiphilic protein that can irreversibly adsorb at the air/water interface. The formed protein monolayers can reach a state of two-dimensional elastic solid that exhibits a high mechanical strength as compared to adsorption layers of typical amphiphilic proteins. Bubbles formed in HFBII solutions preserve the nonspherical shape they had at the moment of solidification of their surfaces. The stirring of HFBII solutions leads to the formation of many bubbles of micrometer size. Measuring the electrophoretic mobility of such bubbles, the Χ-potential was determined. Upon compression, the HFBII monolayers form periodic wrinkles of wavelength 11.5 μm, which corresponds to bending elasticity kc = 1.1 × 10-19 J. The wrinkled hydrophobin monolayers are close to a tension-free state, which prevents the Ostwald ripening and provides bubble longevity in HFBII stabilized foams. Films formed between two bubbles are studied by experiments in a capillary cell. In the absence of added electrolyte, the films are electrostatically stabilized. The appearance of protein aggregates is enhanced with the increase of the HFBII and electrolyte concentrations and at pH close to the isoelectric point. When the aggregate concentration is not too high (to block the film thinning), the films reach a state with 12 nm uniform thickness, which corresponds to two surface monolayers plus HFBII tetramers sandwiched between them. In water, the HFBII molecules can stick to each other not only by their hydrophobic moieties but also by their hydrophilic parts. The latter leads to the attachment of HFBII aggregates such as dimers, tetramers, and bigger ones to the interfacial adsorption monolayers, which provides additional stabilization of the liquid films.

AB - The HFBII hydrophobin is an amphiphilic protein that can irreversibly adsorb at the air/water interface. The formed protein monolayers can reach a state of two-dimensional elastic solid that exhibits a high mechanical strength as compared to adsorption layers of typical amphiphilic proteins. Bubbles formed in HFBII solutions preserve the nonspherical shape they had at the moment of solidification of their surfaces. The stirring of HFBII solutions leads to the formation of many bubbles of micrometer size. Measuring the electrophoretic mobility of such bubbles, the Χ-potential was determined. Upon compression, the HFBII monolayers form periodic wrinkles of wavelength 11.5 μm, which corresponds to bending elasticity kc = 1.1 × 10-19 J. The wrinkled hydrophobin monolayers are close to a tension-free state, which prevents the Ostwald ripening and provides bubble longevity in HFBII stabilized foams. Films formed between two bubbles are studied by experiments in a capillary cell. In the absence of added electrolyte, the films are electrostatically stabilized. The appearance of protein aggregates is enhanced with the increase of the HFBII and electrolyte concentrations and at pH close to the isoelectric point. When the aggregate concentration is not too high (to block the film thinning), the films reach a state with 12 nm uniform thickness, which corresponds to two surface monolayers plus HFBII tetramers sandwiched between them. In water, the HFBII molecules can stick to each other not only by their hydrophobic moieties but also by their hydrophilic parts. The latter leads to the attachment of HFBII aggregates such as dimers, tetramers, and bigger ones to the interfacial adsorption monolayers, which provides additional stabilization of the liquid films.

UR - http://www.scopus.com/inward/record.url?scp=79952612090&partnerID=8YFLogxK

U2 - 10.1021/la104726w

DO - 10.1021/la104726w

M3 - Article

C2 - 21319779

AN - SCOPUS:79952612090

VL - 27

SP - 2382

EP - 2392

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 6

ER -