Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Production and characterization of stable foams with fine bubbles from solutions of hydrophobin HFBII and its mixtures with other proteins
Dimitrova, Lydia M. ; Petkov, Plamen V. ; Kralchevsky, Peter A. ; Stoyanov, Simeon D. ; Pelan, Eddie G. - \ 2017
Colloids and Surfaces. A: Physicochemical and Engineering Aspects 521 (2017). - ISSN 0927-7757 - p. 92 - 104.
Hydrophobins are proteins that are excellent foam stabilizers. We investigated the effects of pH and addition of other proteins on the foaminess, bubble size, and stability of foams from aqueous solutions of the protein HFBII hydrophobin. The produced stable foams have bubbles of radii smaller than 40 μm that obey the lognormal distribution. The overrun of most foams is in the range from 5 to 8, which indicates a good foaminess. The foam longevity is characterized by the time dependences of the foam volume and weight. A combined quantitative criterion for stability, the degree of foam conservation, is proposed. The produced foams are stable for at least 12–17 days. The high foam stability can be explained with the formation of dense hydrophobin adsorption layers, which are impermeable to gas transfer and block the Ostwald ripening (foam disproportionation). In addition, the population of small bubbles formed in the HFBII solutions blocks the drainage of water through the Plateau borders in the foam. The variation of pH does not essentially affect the foaminess and foam stability. The addition of “regular” proteins, such as beta-lactoglobulin, ovalbumin and bovine serum albumin, to the HFBII solutions does not deteriorate the quality and stability of the produced foams up to 94% weight fraction of the added protein. The results and conclusions from the present study could be useful for the applications of hydrophobins as foam stabilizers.
Limited coalescence and Ostwald ripening in emulsions stabilized by hydrophobin HFBII and milk proteins
Dimitrova, Lydia M. ; Boneva, Mariana P. ; Danov, Krassimir D. ; Kralchevsky, Peter A. ; Basheva, Elka S. ; Marinova, Krastanka G. ; Petkov, Jordan T. ; Stoyanov, Simeon D. - \ 2016
Colloids and Surfaces. A: Physicochemical and Engineering Aspects 509 (2016). - ISSN 0927-7757 - p. 521 - 538.
Drop size distribution - Emulsification - Emulsion stability - HFBII hydrophobin - Ostwald ripening

Hydrophobins are proteins isolated from filamentous fungi, which are excellent foam stabilizers, unlike most of the proteins. In the present study, we demonstrate that hydrophobin HFBII can also serve as excellent emulsion stabilizer. The HFBII adsorption layers at the oil/water interface solidify similarly to those at the air/water interface. The thinning of aqueous films sandwiched between two oil phases ends with the formation of a 6 nm thick protein bilayer, just as in the case of foam films, which results in strong adhesive interactions between the emulsion drops. The drop-size distribution in hydrophobin stabilized oil-in-water emulsions is investigated at various protein concentrations and oil volume fractions. The data analysis indicates that the emulsification occurs in the Kolmogorov regime or in the regime of limited coalescence, depending on the experimental conditions. The emulsions with HFBII are very stable – no changes in the drop-size distributions are observed after storage for 50 days. However, these emulsions are unstable upon stirring, when they are subjected to the action of shear stresses. This instability can be removed by covering the drops with a second adsorption layer from a conventional protein, like β-lactoglobulin. The HFBII surface layer is able to suppress the Ostwald ripening in the case when the disperse phase is oil that exhibits a pronounced solubility in water. Hence, the hydrophobin can be used to stabilize microcapsules of fragrances, flavors, colors or preservatives due to its dense adsorption layers that block the transfer of oil molecules.

Shear rheology of hydrophobic adsorption layers at oil/water interfaces and data interpretation in terms of a viscoelastic thixotropic model
Radulova, G.M. ; Danov, K.D. ; Kralchevsky, P.A. ; Petkov, J.T. ; Stoyanov, S.D. - \ 2014
Soft Matter 10 (2014)31. - ISSN 1744-683X - p. 5777 - 5786.
oil-water interface - dependent relaxation-times - class-ii hydrophobin - protein hfbii - hexadecane/water interface - flexible proteins - bubble stability - beta-casein - surface - monolayers
Here, we investigate the surface shear rheology of class II HFBII hydrophobin layers at the oil/water interface. Experiments in two different dynamic regimes, at a fixed rate of strain and oscillations, have been carried out with a rotational rheometer. The rheological data obtained in both regimes comply with the same viscoelastic thixotropic model, which is used to determine the surface shear elasticity and viscosity, Esh and ¿sh. Their values for HFBII at oil/water interfaces are somewhat lower than those at the air/water interface. Moreover, Esh and ¿sh depend on the nature of oil, being smaller for hexadecane in comparison with soybean-oil. It is remarkable that Esh is independent of the rate of strain in the whole investigated range of shear rates. For oil/water interfaces, Esh and ¿sh determined for HFBII layers are considerably greater than for other proteins, like lysozyme and ß-casein. It is confirmed that the hydrophobin forms the most rigid surface layers among all investigated proteins not only for the air/water, but also for the oil/water interface. The wide applicability of the used viscoelastic thixotropic model is confirmed by analyzing data for adsorption layers at oil/water interfaces from lysozyme and ß-casein – both native and cross-linked by enzyme, as well as for films from asphaltene. This model turns out to be a versatile tool for determining the surface shear elasticity and viscosity, Esh and ¿sh, from experimental data for the surface storage and loss moduli, G' and G''.
Sound absorption properties of porous composites fabricated by a hydrogel templating technique
Rutkevicius, M. ; Mehl, G.H. ; Paunov, V.N. ; Qin, Q. ; Rubini, P.A. ; Stoyanov, S.D. ; Petkov, J. - \ 2013
Journal of Materials Research 28 (2013)17. - ISSN 0884-2914 - p. 2409 - 2414.
concrete - porosity
We have used a hydrogel templating technique followed by the subsequent evaporation of water present to fabricate porous cement and porous PDMS composites, and we have analyzed their sound absorption properties. All experiments were carried out with hydrogel slurries of broad bead size distributions. Porous PDMS and cement composites were produced with porosities of up to 80% and 70%, respectively. Scanning electron microscope analysis shows fibrous domains within the voids created by the hydrogel in the cement samples and open pore network in the PDMS composites of initial hydrogel content higher than 70 vol%. Sound absorption was improved with respect to control nonporous samples in all composites with porosities higher than 60 vol%, where an open pore structure was formed. The porous PDMS and porous cement produced by this method show better sound absorption at 200-400 Hz and 1200-1800 Hz frequency ranges when compared with the sound absorption in the intermediate frequencies range between 400 and 1000 Hz.
Wetlands in the Sahel, taking Niger as an example: important for palearctic waterbirds, important for people
Brouwer, J. - \ 2003
In: Ferruginous Duck: From Research to Conservation / Petkov, N, Hughes, B, Gallo-Ursi, U, Sofia, Bulgarije, Slimbridge, UK : BridLife International (Conservation Series 6) - p. 130 - 137.
On the attractiveness of working in a small firm
Mok, A.L. - \ 1985
In: Unattractive work / Kiuranovand, C., Petkov, K., - p. 33 - 45.
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