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20231223074645.0 |
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231223s2005 xx ||||| 00| ||eng c |
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|a pubmed24n0522.xml
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|a (DE-627)NLM156686317
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|a (NLM)16032881
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Murray, Brent S
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Coalescence of protein-stabilized bubbles undergoing expansion at a simultaneously expanding planar air-water interface
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| 264 |
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|c 2005
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 23.06.2006
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|a Date Revised 26.10.2019
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|a published: Print
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|a Citation Status MEDLINE
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|a A novel design of apparatus is described that allows observation of the coalescence stability of bubbles at a planar interface when the planar interface and the bubble surface both expand. Bubbles are introduced beneath the planar air-water interface contained within a square barrier made of perfluorocarbon rubber. The bubbles are then expanded by reducing the air pressure above the interface, while at the same time the rubber barrier is mechanically expanded, maintaining its square shape, to give the same rate and extent of expansion of the planar interface. The area can typically be increased by a factor of three over time scales as short as 0.2 s. This arrangement has been designed to mimic the behavior of aerated products when they exit from a pressurized aeration unit or product dispenser. Compared to results obtained via a previous technique, where it was only possible to expand the bubbles but not the planar interface, the bubbles are less stable. The apparatus has been used to compare the stabilizing effects of ovalbumin, beta-lactoglobulin, whey protein isolate, and sodium caseinate, in a model aqueous food system thickened with 40% invert sugar. Stability improved with increasing concentration of all the proteins and with a decrease in expansion rate, but considerable instability remained even at protein concentrations as high as 4 to 6 wt % and also at very low expansion rates, though the systems were stable in the absence of expansion. However, the stability was greatly improved by the replacement of the above proteins by the hydrocolloids gelatine or polypropylene glycol alginate. Detailed analysis revealed that the coalescence of individual bubbles in clusters of bubbles were not strongly correlated in distance or time, but larger bubbles and bubbles toward the outside of a cluster were found to be, on average, less stable than smaller bubbles and bubbles located more toward the interior of a cluster. The different degrees of stability are discussed in terms of local deformation, fracture behavior, and time-dependent composition of the adsorbed layers
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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|a Lactoglobulins
|2 NLM
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| 650 |
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|a Multiprotein Complexes
|2 NLM
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| 650 |
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|a Proteins
|2 NLM
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| 650 |
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|a Water
|2 NLM
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| 650 |
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|a 059QF0KO0R
|2 NLM
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| 650 |
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|a Ovalbumin
|2 NLM
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| 650 |
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7 |
|a 9006-59-1
|2 NLM
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| 700 |
1 |
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|a Dickinson, Eric
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lau, Cathy Ka
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Nelson, Phillip V
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schmidt, Estelle
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 21(2005), 10 vom: 10. Mai, Seite 4622-30
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:21
|g year:2005
|g number:10
|g day:10
|g month:05
|g pages:4622-30
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|d 21
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|h 4622-30
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