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Characterization of the microstructure of phase segregated amylopectin and beta-lactoglobulin dry mixtures

Quiroga, Carla LU and Bergenståhl, Björn LU (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)
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author
organization
publishing date
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
2008-01-08 15:38:48
date last changed
2017-06-11 03:39:07
@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},
  keyword      = {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},
  volume       = {2},
  year         = {2007},
}