Characterization of the microstructure of phase segregated amylopectin and beta-lactoglobulin dry mixtures
(2007) In Food Biophysics 2(4). p.172-182- Abstract
- The microstructure of phase-segregated amylopectin (AP) and β-lactoglobulin (βlg) mixtures formed during drying from solutions with different concentrations and different polysaccharide and protein ratios have been studied using atomic force microscopy (AFM) and transmission electron microscopy (TEM). AFM was used as the main technique and TEM was used to confirm the results. Systems with only one of the components, AP or βlg, displayed even structures. When the polysaccharide and the protein were in the same system they phase segregated with a sharp boundary between the phases. According to the type of surface morphology of the phase-segregated samples, they were grouped into: domains wetting the air-water surface and domains appearing to... (More)
- The microstructure of phase-segregated amylopectin (AP) and β-lactoglobulin (βlg) mixtures formed during drying from solutions with different concentrations and different polysaccharide and protein ratios have been studied using atomic force microscopy (AFM) and transmission electron microscopy (TEM). AFM was used as the main technique and TEM was used to confirm the results. Systems with only one of the components, AP or βlg, displayed even structures. When the polysaccharide and the protein were in the same system they phase segregated with a sharp boundary between the phases. According to the type of surface morphology of the phase-segregated samples, they were grouped into: domains wetting the air-water surface and domains appearing to be immersed in the solid film. The size range of the domains varied widely from about some nanometers to about a few micrometers which was determined by kinetic reasons or by restrictions given by the film structure of the sample. The two phase systems were AP-continuous phase at AP to βlg ratios above about 1:3 and βlg-continuous phase at ratios below about 1:6. Between these ratios, the systems appeared more or less bicontinuous. The morphology as well as its position in the phase diagram suggested a spinodal phase separation. Phase separation was also observed in the metastable region (AP to βlg ratio 3:1), although the domains were smaller and less developed and it was interpreted as binodal phase separation. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/584966
- author
- Quiroga, Carla LU and Bergenståhl, Björn LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- atomic force microscopy, amylopectin, beta-lactoglobulin, films, dry, spinodal decomposition, phase segregation, polymer incompatibility
- in
- Food Biophysics
- volume
- 2
- issue
- 4
- pages
- 172 - 182
- publisher
- Springer
- external identifiers
-
- scopus:36549090084
- wos:000251092400005
- ISSN
- 1557-1866
- DOI
- 10.1007/s11483-007-9041-8
- language
- English
- LU publication?
- yes
- id
- 690483a6-3b88-4298-8002-b23cf33232e0 (old id 584966)
- date added to LUP
- 2016-04-01 12:07:14
- date last changed
- 2024-01-30 10:28:40
@article{690483a6-3b88-4298-8002-b23cf33232e0,
abstract = {{The microstructure of phase-segregated amylopectin (AP) and β-lactoglobulin (βlg) mixtures formed during drying from solutions with different concentrations and different polysaccharide and protein ratios have been studied using atomic force microscopy (AFM) and transmission electron microscopy (TEM). AFM was used as the main technique and TEM was used to confirm the results. Systems with only one of the components, AP or βlg, displayed even structures. When the polysaccharide and the protein were in the same system they phase segregated with a sharp boundary between the phases. According to the type of surface morphology of the phase-segregated samples, they were grouped into: domains wetting the air-water surface and domains appearing to be immersed in the solid film. The size range of the domains varied widely from about some nanometers to about a few micrometers which was determined by kinetic reasons or by restrictions given by the film structure of the sample. The two phase systems were AP-continuous phase at AP to βlg ratios above about 1:3 and βlg-continuous phase at ratios below about 1:6. Between these ratios, the systems appeared more or less bicontinuous. The morphology as well as its position in the phase diagram suggested a spinodal phase separation. Phase separation was also observed in the metastable region (AP to βlg ratio 3:1), although the domains were smaller and less developed and it was interpreted as binodal phase separation.}},
author = {{Quiroga, Carla and Bergenståhl, Björn}},
issn = {{1557-1866}},
keywords = {{atomic force microscopy; amylopectin; beta-lactoglobulin; films; dry; spinodal decomposition; phase segregation; polymer incompatibility}},
language = {{eng}},
number = {{4}},
pages = {{172--182}},
publisher = {{Springer}},
series = {{Food Biophysics}},
title = {{Characterization of the microstructure of phase segregated amylopectin and beta-lactoglobulin dry mixtures}},
url = {{http://dx.doi.org/10.1007/s11483-007-9041-8}},
doi = {{10.1007/s11483-007-9041-8}},
volume = {{2}},
year = {{2007}},
}