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Competitive protein adsorption between b-casein and b-lactoglobulin during spray-drying: effect of calcium induced association.

Landström, Karin; Arnebrant, T; Alsins, J and Bergenståhl, Björn LU (2003) In Food Hydrocolloids 17(1). p.103-116
Abstract
Competitive adsorption between -casein and -lactoglobulin (-Lg) during spray-drying was studied by the new surface sensitive technique using fluorescence quenching of pyrene labelled protein at the powder surface. The difference in competitiveness of -casein when present as monomers and as associated into micellar like structures were studied. Results were compared with the adsorption of single proteins at the powder surface. The adsorption of monomeric -casein alone gave an apparent surface load of ≈1 mg/m2 at a protein concentration of 0.3% dry weight and then remained constant with an increasing protein concentration. In the presence of Ca2+, associated -casein gave a lower affinity adsorption than monomeric -casein and did not reach a... (More)
Competitive adsorption between -casein and -lactoglobulin (-Lg) during spray-drying was studied by the new surface sensitive technique using fluorescence quenching of pyrene labelled protein at the powder surface. The difference in competitiveness of -casein when present as monomers and as associated into micellar like structures were studied. Results were compared with the adsorption of single proteins at the powder surface. The adsorption of monomeric -casein alone gave an apparent surface load of ≈1 mg/m2 at a protein concentration of 0.3% dry weight and then remained constant with an increasing protein concentration. In the presence of Ca2+, associated -casein gave a lower affinity adsorption than monomeric -casein and did not reach a plateau value, instead it continued to increase with an increasing protein concentration. -Lg showed a low-affinity adsorption during spray-drying compared to monomeric -casein, although not as low as associated -casein. Competitive adsorption between monomeric -casein and -Lg resulted in a higher apparent surface load of -casein than -Lg at both protein concentrations studied (total 0.3 and 3.3% dry weight). However, in an associated form -casein was less competitive than -Lg. At a low bulk protein concentration (0.3% dry weight) -Lg dominated the powder surface, whereas at a higher concentration (3.3% dry weight) there was little difference between the proteins. The results indicate that the competitiveness of a protein during spray-drying is highly influenced by the ability of the protein to attach and rearrange at the droplet's air–water interface during the spray-drying process. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Fluorescence quenching, Pyrene, β-Lactoglobulin, β-Casein, Competitive protein adsorption, Calcium, Spray-drying
in
Food Hydrocolloids
volume
17
issue
1
pages
103 - 116
publisher
Elsevier
external identifiers
  • wos:000180610700009
  • scopus:0037240233
ISSN
0268-005X
DOI
10.1016/S0268-005X(02)00044-9
language
English
LU publication?
yes
id
05346db6-c037-4191-a0eb-281c4e46f35b (old id 128276)
date added to LUP
2007-07-18 15:31:19
date last changed
2017-01-01 07:35:49
@article{05346db6-c037-4191-a0eb-281c4e46f35b,
  abstract     = {Competitive adsorption between -casein and -lactoglobulin (-Lg) during spray-drying was studied by the new surface sensitive technique using fluorescence quenching of pyrene labelled protein at the powder surface. The difference in competitiveness of -casein when present as monomers and as associated into micellar like structures were studied. Results were compared with the adsorption of single proteins at the powder surface. The adsorption of monomeric -casein alone gave an apparent surface load of ≈1 mg/m2 at a protein concentration of 0.3% dry weight and then remained constant with an increasing protein concentration. In the presence of Ca2+, associated -casein gave a lower affinity adsorption than monomeric -casein and did not reach a plateau value, instead it continued to increase with an increasing protein concentration. -Lg showed a low-affinity adsorption during spray-drying compared to monomeric -casein, although not as low as associated -casein. Competitive adsorption between monomeric -casein and -Lg resulted in a higher apparent surface load of -casein than -Lg at both protein concentrations studied (total 0.3 and 3.3% dry weight). However, in an associated form -casein was less competitive than -Lg. At a low bulk protein concentration (0.3% dry weight) -Lg dominated the powder surface, whereas at a higher concentration (3.3% dry weight) there was little difference between the proteins. The results indicate that the competitiveness of a protein during spray-drying is highly influenced by the ability of the protein to attach and rearrange at the droplet's air–water interface during the spray-drying process.},
  author       = {Landström, Karin and Arnebrant, T and Alsins, J and Bergenståhl, Björn},
  issn         = {0268-005X},
  keyword      = {Fluorescence quenching,Pyrene,β-Lactoglobulin,β-Casein,Competitive protein adsorption,Calcium,Spray-drying},
  language     = {eng},
  number       = {1},
  pages        = {103--116},
  publisher    = {Elsevier},
  series       = {Food Hydrocolloids},
  title        = {Competitive protein adsorption between b-casein and b-lactoglobulin during spray-drying: effect of calcium induced association.},
  url          = {http://dx.doi.org/10.1016/S0268-005X(02)00044-9},
  volume       = {17},
  year         = {2003},
}