Shear rheology of mixed protein adsorption layers vs their structure studied by surface force measurements

Danov, Krassimir D.; Kralchevsky, Peter A.; Radulova, Gergana M.; Basheva, Elka S.; Stoyanov, Simeon D.; Pelan, Eddie G.

doi:10.1016/j.cis.2014.04.009

Cited by 24 publications

(38 citation statements)

References 59 publications

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“…Thus, a particular class I or class II hydrophobin can be chosen depending on the requirements of the application. Biophysical and biochemical properties of hydrophobin films can be optimized by genetic engineering Lahtinen et al 2008;Joensuu et al 2010) or by adding surfactants (Morris et al 2011;Zhang et al 2011a, b, c;Tucker et al 2014), glycans (Scholtmeijer et al 2009), or other proteins (Danov et al 2014) …”

Section: Resultsmentioning

confidence: 99%

Applications of hydrophobins: current state and perspectives

Wösten

Scholtmeijer

2015

Appl Microbiol Biotechnol

140

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Hydrophobins are proteins exclusively produced by filamentous fungi. They self-assemble at hydrophilichydrophobic interfaces into an amphipathic film. This protein film renders hydrophobic surfaces of gas bubbles, liquids, or solid materials wettable, while hydrophilic surfaces can be turned hydrophobic. These properties, among others, make hydrophobins of interest for medical and technical applications. For instance, hydrophobins can be used to disperse hydrophobic materials; to stabilize foam in food products; and to immobilize enzymes, peptides, antibodies, cells, and anorganic molecules on surfaces. At the same time, they may be used to prevent binding of molecules. Furthermore, hydrophobins have therapeutic value as immunomodulators and can been used to produce recombinant proteins.

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Section: Resultsmentioning

confidence: 99%

Applications of hydrophobins: current state and perspectives

Wösten

Scholtmeijer

2015

Appl Microbiol Biotechnol

140

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“…At an air/water or oil/water interface, the adsorption layer of HFBII fast solidifies, i.e. it acquires surface shear elasticity, which is higher than that measured for all other investigated proteins [10,[26][27][28][29][30]. The hydrophobin adsorption layers possess also a high dilatational elasticity and the hydrophobin adsorption at the air/water interface is irreversible [31][32][33][34][35][36].…”

Section: Introductionmentioning

confidence: 91%

Production and characterization of stable foams with fine bubbles from solutions of hydrophobin HFBII and its mixtures with other proteins

Dimitrova

Petkov

Kralchevsky

et al. 2017

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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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.

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“…Hägerström et al [26] also found that bovine submaxillary gland mucin destroyed the interfacial network structure of the absorbed deacetylated gellan gum. Danov et al [28] observed the same phenomena for the interfacial properties of active globular protein hydrophobin (HFBII) and the disordering protein β-casein. They showed that the disordering protein decreases the rigidity of the HFBII adsorption layers, due to the penetration of long hydrophobic chains of β-casein between the adsorbed HFBII molecules, as driven by the favorable hydrophobic interaction between the chains and air.…”

Section: Time Dependence Of the Interfacial Modulusmentioning

confidence: 66%

Interfacial shear rheology of β-lactoglobulin—Bovine submaxillary mucin layers adsorbed at air/water interface

Çelebioğlu

Kmiecik-Palczewska

Lee

et al. 2017

International Journal of Biological Macromolecules

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The interfacial rheological properties of solutions of β-lactoglobulin (BLG), as a model food compound, mixed with bovine submaxillary mucin (BSM), a major salivary protein, have been investigated. Time, frequency, stress sweep and flow measurements have been performed at different pHs (7.4, 5.0 and 3.0), to investigate the air/water interfacial properties. All protein layers (BLG, BSM, and BLG-BSM mixtures) formed an elastic network at the air/water interface with low frequency dependence of the interfacial modulus. The results indicated that BLG moves faster as smaller molecule than mucin, and dominate the surface adsorption and the network formation for the BLG-BSM mixtures. Moreover, BLG-BSM protein mixtures exhibited interfacial properties with lower elastic and viscous moduli than BLG, as a result of competitive displacement of BLG proteins with BSMs from the interface. It is suggested that hydrophobic patches of BSM can be imbedded into the BLG monolayer as driven by a strong hydrophobic interaction with air and disrupt the cohesive assembly of BLG, whereas the hydrophilic (negatively charged) parts of the BSM chain are protruding from the interface towards the bulk water.

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Shear rheology of mixed protein adsorption layers vs their structure studied by surface force measurements

Cited by 24 publications

References 59 publications

Applications of hydrophobins: current state and perspectives

Applications of hydrophobins: current state and perspectives

Production and characterization of stable foams with fine bubbles from solutions of hydrophobin HFBII and its mixtures with other proteins

Interfacial shear rheology of β-lactoglobulin—Bovine submaxillary mucin layers adsorbed at air/water interface

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