Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Elka S. Basheva"'
Publikováno v:
Materials, Vol 9, Iss 3, p 145 (2016)
Experimental data for the disjoining pressure of foam films stabilized by anionic surfactant in the presence of 1:1, 1:2, 1:3, and 2:2 electrolytes: NaCl, Na2SO4, Na3Citrate, and MgSO4 are reported. The disjoining pressure predicted by the Derjaguin-
Externí odkaz:
https://doaj.org/article/defa219827314571a63e9ccd20bdf242
Autor:
Krassimir D. Danov, Peter A. Kralchevsky, Rumyana D. Stanimirova, Elka S. Basheva, Jordan T. Petkov, Neil Shaw
Publikováno v:
Journal of Colloid and Interface Science. 576:345-355
Hypothesis: New dynamic phenomena can be observed in evaporating free liquid films from colloidal solutions with bimodal particle size distribution. Such distributions are formed in a natural way in mixed (slightly turbid) solutions of cationic and a
Autor:
Yee Wei Ung, Veronika I. Yavrukova, Gergana M. Radulova, Elka S. Basheva, Rumyana D. Stanimirova, Jordan T. Petkov, Peter A. Kralchevsky, Krassimir D. Danov, Hui Xu, Emily H. P. Tan
Publikováno v:
Proceedings of the Virtual 2021 AOCS Annual Meeting & Expo.
Autor:
Yee Wei Ung, Peter A. Kralchevsky, Elka S. Basheva, Hui Xu, Jordan T. Petkov, Gergana M. Radulova, Krassimir D. Danov
Publikováno v:
Journal of Colloid and Interface Science
Hypotheses The micellar solutions of sulfonated methyl esters (SME) are expected to form stratifying foam films that exhibit stepwise thinning. From the height of the steps, which are engendered by micellar layers confined in the films, we could dete
Autor:
Tatiana G. Slavova, Krassimir D. Danov, Krastanka G. Marinova, Gergana M. Radulova, Elka S. Basheva, Peter A. Kralchevsky
Publikováno v:
Colloids and Surfaces A: Physicochemical and Engineering Aspects. 559:351-364
Colloidosomes provide a possibility to encapsulate oily substances in water in the form of core-in-shell structures. In this study, we produced microcapsules with shell from colloidal particles, where the interparticle openings are blocked by mixed l
Autor:
Erqiang Li, Ivan U. Vakarelski, Sigurdur T. Thoroddsen, Elka S. Basheva, Derek Y. C. Chan, Rogerio Manica
Publikováno v:
Langmuir. 34:2096-2108
Coalescence dynamics between deformable bubbles and droplets can be dramatically affected by the mobility of the interfaces with fully tangentially mobile bubble-liquid or droplet-liquid interfaces expected to accelerate the coalescence by orders of
Autor:
Eddie G. Pelan, Gergana M. Radulova, Simeon D. Stoyanov, Elka S. Basheva, Krassimir D. Danov, Peter A. Kralchevsky
Publikováno v:
Advances in Colloid and Interface Science, 222, 148-161
Advances in Colloid and Interface Science 222 (2015)
Advances in Colloid and Interface Science 222 (2015)
The hydrophobins are proteins that form the most rigid adsorption layers at liquid interfaces in comparison with all other investigated proteins. The mixing of hydrophobin HFBII with other conventional proteins is expected to reduce the surface shear
Publikováno v:
Current Opinion in Colloid & Interface Science. 16:517-524
article i nfo Experiments with foam films from solutions of 1 mM SDS+100 mM electrolyte (LiCl, NaCl and CsCl) were carried out by a thin-film-pressure balance. The measured dependences of disjoining pressure versus film thickness exhibit a steep incr
Autor:
Krassimir D. Danov, Alex Lips, Kavssery P. Ananthapadmanabhan, Peter A. Kralchevsky, Elka S. Basheva
Publikováno v:
Advances in Colloid and Interface Science. 168:50-70
The stepwise thinning (stratification) of liquid films containing electrically charged colloidal particles (in our case - surfactant micelles) is investigated. Most of the results are applicable also to films from nanoparticle suspensions. The aim is
Autor:
Simeon D. Stoyanov, Theo B. J. Blijdenstein, Alex Lips, Krassimir D. Danov, Eddie G. Pelan, Elka S. Basheva, Peter A. Kralchevsky
Publikováno v:
Langmuir. 27:4481-4488
The hydrophobins are a class of amphiphilic proteins which spontaneously adsorb at the air/water interface and form elastic membranes of high mechanical strength as compared to other proteins. The mechanism of hydrophobin adhesion is of interest for