Advanced

Interaction between cereal β-glucan and proteins in solution and at interfaces

Zielke, Claudia LU ; Lu, Yi LU ; Poinsot, Romane and Nilsson, Lars LU (2018) In Colloids and Surfaces B: Biointerfaces 162. p.256-264
Abstract

Cereal β-glucan is well known for its beneficial health effects, such as lowering of blood cholesterol values and a reduced risk of coronary heart disease. These effects are often discussed in relation to the dissolution and aggregation behavior of the β-glucan during human digestion. Furthermore, potential proteinaceous material present is believed to have an important impact on the formation of viscous slurries during digestion and might influence the aggregation behavior of the β-glucan. Therefore, the interaction and aggregation behavior of a β-glucan isolate (OBC90) with two different proteins (gliadin and whey protein) was investigated in solution at different pH with regards to kinetics of aggregation and protein/β-glucan ratio... (More)

Cereal β-glucan is well known for its beneficial health effects, such as lowering of blood cholesterol values and a reduced risk of coronary heart disease. These effects are often discussed in relation to the dissolution and aggregation behavior of the β-glucan during human digestion. Furthermore, potential proteinaceous material present is believed to have an important impact on the formation of viscous slurries during digestion and might influence the aggregation behavior of the β-glucan. Therefore, the interaction and aggregation behavior of a β-glucan isolate (OBC90) with two different proteins (gliadin and whey protein) was investigated in solution at different pH with regards to kinetics of aggregation and protein/β-glucan ratio and at interfaces. Aggregates were found at low pH and the aggregation and composition of aggregates seems to depend on the type of protein. Furthermore, phosphate was found at low concentrations in the β-glucan, most likely being the reason for the net negative charge at pH ≤ 4. Therefore, electrostatic interaction is suggested to play an important role for the aggregation between β-glucan and proteins.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Asymmetric flow field-flow fractionation (AF4), Differential refractive index (dRI), Electrostatic interaction, Ellipsometry, Gliadin, Multi-angle light scattering (MALS), Natural phosphate, Polysaccharide, Transmission, Whey protein (WP)
in
Colloids and Surfaces B: Biointerfaces
volume
162
pages
9 pages
publisher
Elsevier
external identifiers
  • scopus:85036468302
ISSN
0927-7765
DOI
10.1016/j.colsurfb.2017.11.059
language
English
LU publication?
yes
id
97b6e26c-4bf5-4847-b16d-c60cc54149bc
date added to LUP
2017-12-14 07:23:23
date last changed
2018-05-29 10:04:27
@article{97b6e26c-4bf5-4847-b16d-c60cc54149bc,
  abstract     = {<p>Cereal β-glucan is well known for its beneficial health effects, such as lowering of blood cholesterol values and a reduced risk of coronary heart disease. These effects are often discussed in relation to the dissolution and aggregation behavior of the β-glucan during human digestion. Furthermore, potential proteinaceous material present is believed to have an important impact on the formation of viscous slurries during digestion and might influence the aggregation behavior of the β-glucan. Therefore, the interaction and aggregation behavior of a β-glucan isolate (OBC90) with two different proteins (gliadin and whey protein) was investigated in solution at different pH with regards to kinetics of aggregation and protein/β-glucan ratio and at interfaces. Aggregates were found at low pH and the aggregation and composition of aggregates seems to depend on the type of protein. Furthermore, phosphate was found at low concentrations in the β-glucan, most likely being the reason for the net negative charge at pH ≤ 4. Therefore, electrostatic interaction is suggested to play an important role for the aggregation between β-glucan and proteins.</p>},
  author       = {Zielke, Claudia and Lu, Yi and Poinsot, Romane and Nilsson, Lars},
  issn         = {0927-7765},
  keyword      = {Asymmetric flow field-flow fractionation (AF4),Differential refractive index (dRI),Electrostatic interaction,Ellipsometry,Gliadin,Multi-angle light scattering (MALS),Natural phosphate,Polysaccharide,Transmission,Whey protein (WP)},
  language     = {eng},
  month        = {02},
  pages        = {256--264},
  publisher    = {Elsevier},
  series       = {Colloids and Surfaces B: Biointerfaces},
  title        = {Interaction between cereal β-glucan and proteins in solution and at interfaces},
  url          = {http://dx.doi.org/10.1016/j.colsurfb.2017.11.059},
  volume       = {162},
  year         = {2018},
}