Complex formation in aqueous medium of partially hydrolysed oat cereal proteins with sodium stearoyl-2 lactylate (SSL) lipid surfactant and implications for bile acids activity
(2004) In Colloids and Surfaces B: Biointerfaces 35(3-4). p.175-184- Abstract
- Sodium stearoyl-2 lactylate (SSL) lipid surfactant molecules specifically bind partially hydrolysed oat proteins in aqueous medium and significantly enhance the dispersion stability of oat cereal preparations. The proposed complexation is composition dependent and a greater understanding of the role of both oat proteins and lipid surfactant in the effect was gained with data from high performance liquid chromatography (HPLC-UV), viscometry and differential scanning micro calorimetry. The effect of the lipid surfactant on the degree of association is primarily governed by the conformational activity of oat protein molecules related to the extent of protein hydrolysed state, as well as protein unfolded and subsequent aggregated structures.... (More)
- Sodium stearoyl-2 lactylate (SSL) lipid surfactant molecules specifically bind partially hydrolysed oat proteins in aqueous medium and significantly enhance the dispersion stability of oat cereal preparations. The proposed complexation is composition dependent and a greater understanding of the role of both oat proteins and lipid surfactant in the effect was gained with data from high performance liquid chromatography (HPLC-UV), viscometry and differential scanning micro calorimetry. The effect of the lipid surfactant on the degree of association is primarily governed by the conformational activity of oat protein molecules related to the extent of protein hydrolysed state, as well as protein unfolded and subsequent aggregated structures. SSL does not dissociate oat proteins into subunits or destroy important hydrophobic contacts already stabilising the protein molecules. Although the exact mode of association is unknown, the present study demonstrates that such interactions occur in a specific manner and suggest selectivity of oat proteins for individual fatty acids. The effect of various amounts of bile acids on SSL-oat protein interaction was also investigated, as a first attempt to investigate the role of lipid surfactant molecules in the known cholesterol-lowering action of oat cereal ingredients and to elucidate favourable conditions by which oat cereal can elicit hypocholesterolemic effects. (C) 2004 Elsevier B.V. All rights reserved. (Less)
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https://lup.lub.lu.se/record/138617
- author
- Chronakis, I S ; Fredholm, A ; Öste Triantafyllou, A and Öste, Rickard LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Oat cereal protein, SSL lipid surfactant, Interactions, Bile acids
- in
- Colloids and Surfaces B: Biointerfaces
- volume
- 35
- issue
- 3-4
- pages
- 175 - 184
- publisher
- Elsevier
- external identifiers
-
- pmid:15261029
- wos:000222172100005
- scopus:2542484369
- ISSN
- 1873-4367
- DOI
- 10.1016/j.colsurfb.2004.03.011
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Applied Nutrition and Food Chemistry (011001300)
- id
- 8e422afd-2ae6-40ab-b180-e858fb3ff518 (old id 138617)
- date added to LUP
- 2016-04-01 16:51:15
- date last changed
- 2023-09-05 02:34:14
@article{8e422afd-2ae6-40ab-b180-e858fb3ff518,
abstract = {{Sodium stearoyl-2 lactylate (SSL) lipid surfactant molecules specifically bind partially hydrolysed oat proteins in aqueous medium and significantly enhance the dispersion stability of oat cereal preparations. The proposed complexation is composition dependent and a greater understanding of the role of both oat proteins and lipid surfactant in the effect was gained with data from high performance liquid chromatography (HPLC-UV), viscometry and differential scanning micro calorimetry. The effect of the lipid surfactant on the degree of association is primarily governed by the conformational activity of oat protein molecules related to the extent of protein hydrolysed state, as well as protein unfolded and subsequent aggregated structures. SSL does not dissociate oat proteins into subunits or destroy important hydrophobic contacts already stabilising the protein molecules. Although the exact mode of association is unknown, the present study demonstrates that such interactions occur in a specific manner and suggest selectivity of oat proteins for individual fatty acids. The effect of various amounts of bile acids on SSL-oat protein interaction was also investigated, as a first attempt to investigate the role of lipid surfactant molecules in the known cholesterol-lowering action of oat cereal ingredients and to elucidate favourable conditions by which oat cereal can elicit hypocholesterolemic effects. (C) 2004 Elsevier B.V. All rights reserved.}},
author = {{Chronakis, I S and Fredholm, A and Öste Triantafyllou, A and Öste, Rickard}},
issn = {{1873-4367}},
keywords = {{Oat cereal protein; SSL lipid surfactant; Interactions; Bile acids}},
language = {{eng}},
number = {{3-4}},
pages = {{175--184}},
publisher = {{Elsevier}},
series = {{Colloids and Surfaces B: Biointerfaces}},
title = {{Complex formation in aqueous medium of partially hydrolysed oat cereal proteins with sodium stearoyl-2 lactylate (SSL) lipid surfactant and implications for bile acids activity}},
url = {{http://dx.doi.org/10.1016/j.colsurfb.2004.03.011}},
doi = {{10.1016/j.colsurfb.2004.03.011}},
volume = {{35}},
year = {{2004}},
}