Competitive adsorption between beta-casein or beta-lactoglobulin and model milk membrane lipids at oil-water interfaces
(2005) In Journal of Agricultural and Food Chemistry 53(3). p.716-724- Abstract
- This study investigated the competitive adsorption between milk proteins and model milk membrane lipids at the oil-water interface and its dependence on the state of the lipid dispersion and the formation of emulsions. Both protein and membrane lipid surface load were determined using a serum depletion technique. The membrane lipid mixture used was a model milk membrane lipid system, containing dioleoylphosphatidylcholine, dioleoylphosphatidylethanolamine, milk sphingomyelin, dioleoylphosphatidylserine, and soybean phosphatidylinositol. The model composition mimics the lipid composition of natural milk fat globule membranes. The interactions were studied for two proteins, beta-lactoglobulin and P-casein. The mixing order was varied to... (More)
- This study investigated the competitive adsorption between milk proteins and model milk membrane lipids at the oil-water interface and its dependence on the state of the lipid dispersion and the formation of emulsions. Both protein and membrane lipid surface load were determined using a serum depletion technique. The membrane lipid mixture used was a model milk membrane lipid system, containing dioleoylphosphatidylcholine, dioleoylphosphatidylethanolamine, milk sphingomyelin, dioleoylphosphatidylserine, and soybean phosphatidylinositol. The model composition mimics the lipid composition of natural milk fat globule membranes. The interactions were studied for two proteins, beta-lactoglobulin and P-casein. The mixing order was varied to allow for differentiation between equilibrium structures and nonequilibrium structures. The results showed more than monolayer adsorption for most combinations. Proteins dominated at the oil-water interface in the protein-emulsified emulsion even after 48 h of exposure to a vesicular dispersion of membrane lipids. The membrane lipids dominated the oil-water interface in the case of the membrane lipid emulsified emulsion even after equilibration with a protein solution. Protein displacement with time was observed only for emulsions in which both membrane lipids and beta-casein were included during the emulsification, This study shows that kinetics controls the structures rather than the thermodynamic equilibrium, possibly resulting in structures more complex than an adsorbed monolayer. Thus, it can be expected that procedures such as the mixing order during emulsion preparation are of crucial importance to the emulsification performance. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/152868
- author
- Waninge, Rianne LU ; Walstra, P ; Bastiaans, J ; Nieuwenhuijse, H ; Nylander, Tommy LU ; Paulsson, Marie LU and Bergenståhl, Björn LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Agricultural and Food Chemistry
- volume
- 53
- issue
- 3
- pages
- 716 - 724
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000226782900034
- pmid:15686425
- scopus:13244271973
- pmid:15686425
- ISSN
- 0021-8561
- DOI
- 10.1021/jf049267y
- language
- English
- LU publication?
- yes
- id
- 2f671bb0-33da-4bae-88ba-5b264698608c (old id 152868)
- date added to LUP
- 2016-04-01 11:34:20
- date last changed
- 2023-11-10 17:06:17
@article{2f671bb0-33da-4bae-88ba-5b264698608c,
abstract = {{This study investigated the competitive adsorption between milk proteins and model milk membrane lipids at the oil-water interface and its dependence on the state of the lipid dispersion and the formation of emulsions. Both protein and membrane lipid surface load were determined using a serum depletion technique. The membrane lipid mixture used was a model milk membrane lipid system, containing dioleoylphosphatidylcholine, dioleoylphosphatidylethanolamine, milk sphingomyelin, dioleoylphosphatidylserine, and soybean phosphatidylinositol. The model composition mimics the lipid composition of natural milk fat globule membranes. The interactions were studied for two proteins, beta-lactoglobulin and P-casein. The mixing order was varied to allow for differentiation between equilibrium structures and nonequilibrium structures. The results showed more than monolayer adsorption for most combinations. Proteins dominated at the oil-water interface in the protein-emulsified emulsion even after 48 h of exposure to a vesicular dispersion of membrane lipids. The membrane lipids dominated the oil-water interface in the case of the membrane lipid emulsified emulsion even after equilibration with a protein solution. Protein displacement with time was observed only for emulsions in which both membrane lipids and beta-casein were included during the emulsification, This study shows that kinetics controls the structures rather than the thermodynamic equilibrium, possibly resulting in structures more complex than an adsorbed monolayer. Thus, it can be expected that procedures such as the mixing order during emulsion preparation are of crucial importance to the emulsification performance.}},
author = {{Waninge, Rianne and Walstra, P and Bastiaans, J and Nieuwenhuijse, H and Nylander, Tommy and Paulsson, Marie and Bergenståhl, Björn}},
issn = {{0021-8561}},
language = {{eng}},
number = {{3}},
pages = {{716--724}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of Agricultural and Food Chemistry}},
title = {{Competitive adsorption between beta-casein or beta-lactoglobulin and model milk membrane lipids at oil-water interfaces}},
url = {{http://dx.doi.org/10.1021/jf049267y}},
doi = {{10.1021/jf049267y}},
volume = {{53}},
year = {{2005}},
}