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Heat induced aggregation of b-lactoglobulin studied by dynamic light scattering

Elofsson, Ulla M.; Dejmek, Petr LU and Paulsson, Marie A. (1996) In International Dairy Journal 6(4). p.343-357
Abstract
The in situ heat-induced aggregation of commercial β-lactoglobulin as such, or after further purification, was followed to a z-average hydrodynamic diameter of 15–20 nm at 59–63 °C by dynamic light scattering. In this temperature range, measurable increase of hydrodynamic diameter occurred after an apparent lag period, which was strongly dependent on heating temperature, pH and initial protein concentration. The changes in time scale of the aggregation process agreed with changes in amount of unfolded β-lactoglobulin, assuming a two-state model of the denaturation. The pH dependence reflected the midpoint unfolding temperature and not the sulphydryl group reactivity, suggesting that this reactivity was not rate limiting in the aggregation.... (More)
The in situ heat-induced aggregation of commercial β-lactoglobulin as such, or after further purification, was followed to a z-average hydrodynamic diameter of 15–20 nm at 59–63 °C by dynamic light scattering. In this temperature range, measurable increase of hydrodynamic diameter occurred after an apparent lag period, which was strongly dependent on heating temperature, pH and initial protein concentration. The changes in time scale of the aggregation process agreed with changes in amount of unfolded β-lactoglobulin, assuming a two-state model of the denaturation. The pH dependence reflected the midpoint unfolding temperature and not the sulphydryl group reactivity, suggesting that this reactivity was not rate limiting in the aggregation. The aggregation process was modelled numerically with FuchsSmoluchowski kinetics. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
International Dairy Journal
volume
6
issue
4
pages
343 - 357
publisher
Elsevier
external identifiers
  • Scopus:0030118518
ISSN
0958-6946
DOI
10.1016/0958-6946(95)00019-4
language
English
LU publication?
yes
id
cc1a1cfb-e6c1-46bc-a9e2-3f59e2820824 (old id 32857)
date added to LUP
2007-06-19 14:31:54
date last changed
2016-10-13 04:37:12
@misc{cc1a1cfb-e6c1-46bc-a9e2-3f59e2820824,
  abstract     = {The in situ heat-induced aggregation of commercial β-lactoglobulin as such, or after further purification, was followed to a z-average hydrodynamic diameter of 15–20 nm at 59–63 °C by dynamic light scattering. In this temperature range, measurable increase of hydrodynamic diameter occurred after an apparent lag period, which was strongly dependent on heating temperature, pH and initial protein concentration. The changes in time scale of the aggregation process agreed with changes in amount of unfolded β-lactoglobulin, assuming a two-state model of the denaturation. The pH dependence reflected the midpoint unfolding temperature and not the sulphydryl group reactivity, suggesting that this reactivity was not rate limiting in the aggregation. The aggregation process was modelled numerically with FuchsSmoluchowski kinetics.},
  author       = {Elofsson, Ulla M. and Dejmek, Petr and Paulsson, Marie A.},
  issn         = {0958-6946},
  language     = {eng},
  number       = {4},
  pages        = {343--357},
  publisher    = {ARRAY(0xc5b62d8)},
  series       = {International Dairy Journal},
  title        = {Heat induced aggregation of b-lactoglobulin studied by dynamic light scattering},
  url          = {http://dx.doi.org/10.1016/0958-6946(95)00019-4},
  volume       = {6},
  year         = {1996},
}