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231224s2016 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.6b00446
|2 doi
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|a pubmed25n0863.xml
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|a (DE-627)NLM259062006
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|a (NLM)27043221
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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 Wan, Zhili
|e verfasserin
|4 aut
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| 245 |
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|a Nonlinear Surface Dilatational Rheology and Foaming Behavior of Protein and Protein Fibrillar Aggregates in the Presence of Natural Surfactant
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|c 2016
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 23.06.2017
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|a Date Revised 13.12.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The surface and foaming properties of native soy glycinin (11S) and its heat-induced fibrillar aggregates, in the presence of natural surfactant steviol glycoside (STE), were investigated and compared at pH 7.0 to determine the impact of protein structure modification on protein-surfactant interfacial interactions. The adsorption at, and nonlinear dilatational rheological behavior of, the air-water interface were studied by combining drop shape analysis tensiometry, ellipsometry, and large-amplitude oscillatory dilatational rheology. Lissajous plots of surface pressure versus deformation were used to analyze the surface rheological response in terms of interfacial microstructure. The heat treatment generates a mixture of long fibrils and unconverted peptides. The presence of small peptides in 11S fibril samples resulted in a faster adsorption kinetics than that of native 11S. The addition of STE affected the adsorption of 11S significantly, whereas no apparent effect on the adsorption of the 11S fibril-peptide system was observed. The rheological response of interfaces stabilized by 11S-STE mixtures also differed significantly from the response for 11S fibril-peptide-STE mixtures. For 11S, the STE reduces the degree of strain hardening in extension and increases strain hardening in compression, suggesting the interfacial structure may change from a surface gel to a mixed phase of protein patches and STE domains. The foams generated from the mixtures displayed comparable foam stability to that of pure 11S. For 11S fibril-peptide mixtures STE only significantly affects the response in extension, where the degree of strain softening is decreased compared to the pure fibril-peptide system. The foam stability of the fibril-peptide system was significantly reduced by STE. These findings indicate that fibrillization of globular proteins could be a potential strategy to modify the complex surface and foaming behaviors of protein-surfactant mixtures
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Diterpenes, Kaurane
|2 NLM
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|a Globulins
|2 NLM
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|a Glucosides
|2 NLM
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|a Protein Aggregates
|2 NLM
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|a Soybean Proteins
|2 NLM
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|a Surface-Active Agents
|2 NLM
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| 650 |
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|a stevioside
|2 NLM
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| 650 |
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|a 0YON5MXJ9P
|2 NLM
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| 650 |
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|a glycinin
|2 NLM
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| 650 |
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|a 9007-93-6
|2 NLM
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| 650 |
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|a rebaudioside A
|2 NLM
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| 650 |
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|a B3FUD0528F
|2 NLM
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| 700 |
1 |
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|a Yang, Xiaoquan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Sagis, Leonard M C
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 32(2016), 15 vom: 19. Apr., Seite 3679-90
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:32
|g year:2016
|g number:15
|g day:19
|g month:04
|g pages:3679-90
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| 856 |
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|u http://dx.doi.org/10.1021/acs.langmuir.6b00446
|3 Volltext
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|h 3679-90
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