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Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry

Paulsson, Marie LU orcid and Dejmek, Petr LU orcid (1990) In Journal of Dairy Science 73(3). p.590-600
Abstract
Thermal
unfolding of whey proteins and whey protein-casein mixtures in simulated
milk ultrafiltrate was studied by differential scanning calorimetry.
The results are reported as transition enthalpy, temperature of peak
maximum, and van’t Hoff enthalpy related to the sharpness of transition.
The results of earlier investigations were reviewed. It is suggested
that a large part of reported whey protein unfolding data are affected
by subsequent aggregation reactions.
Pure
caseins showed no endotherms on heating. In mixtures of whey proteins
and individual caseins, β-casein showed no effect. Addition of 5%
α-casein to 5%... (More)
Thermal
unfolding of whey proteins and whey protein-casein mixtures in simulated
milk ultrafiltrate was studied by differential scanning calorimetry.
The results are reported as transition enthalpy, temperature of peak
maximum, and van’t Hoff enthalpy related to the sharpness of transition.
The results of earlier investigations were reviewed. It is suggested
that a large part of reported whey protein unfolding data are affected
by subsequent aggregation reactions.
Pure
caseins showed no endotherms on heating. In mixtures of whey proteins
and individual caseins, β-casein showed no effect. Addition of 5%
α-casein to 5% whey protein lowered the denaturation temperature of all
whey proteins by 2 to 3°C. κ-Casein did not affect the denaturation
behavior of bovine serum albumin and α-lactalbumin, but it lowered the
denaturation temperature of β-lactoglobulin by 3°C. In the pH range from
6.4 to 7, where the whey protein casein interaction is known to change
drastically in highly heated milk, no abrupt changes are seen in thermal
unfolding of β-lactoglobulin, either alone or in mixture with κ-casein.
(Less)
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author
and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Dairy Science
volume
73
issue
3
pages
11 pages
publisher
American Dairy Science Association
external identifiers
  • scopus:0345436424
ISSN
1525-3198
DOI
10.3168/jds.S0022-0302(90)78707-3
language
English
LU publication?
yes
id
339ce43b-3ce4-440b-83a1-ed58db28550f
date added to LUP
2025-09-19 10:29:09
date last changed
2025-10-14 11:16:17
@article{339ce43b-3ce4-440b-83a1-ed58db28550f,
  abstract     = {{<div><div class="u-margin-s-bottom">Thermal <br>
unfolding of whey proteins and whey protein-casein mixtures in simulated<br>
 milk ultrafiltrate was studied by differential scanning calorimetry. <br>
The results are reported as transition enthalpy, temperature of peak <br>
maximum, and van’t Hoff enthalpy related to the sharpness of transition.<br>
 The results of earlier investigations were reviewed. It is suggested <br>
that a large part of reported whey protein unfolding data are affected <br>
by subsequent aggregation reactions.</div><div class="u-margin-s-bottom">Pure<br>
 caseins showed no endotherms on heating. In mixtures of whey proteins <br>
and individual caseins, β-casein showed no effect. Addition of 5% <br>
α-casein to 5% whey protein lowered the denaturation temperature of all <br>
whey proteins by 2 to 3°C. κ-Casein did not affect the denaturation <br>
behavior of bovine serum albumin and α-lactalbumin, but it lowered the <br>
denaturation temperature of β-lactoglobulin by 3°C. In the pH range from<br>
 6.4 to 7, where the whey protein casein interaction is known to change <br>
drastically in highly heated milk, no abrupt changes are seen in thermal<br>
 unfolding of β-lactoglobulin, either alone or in mixture with κ-casein.</div></div>}},
  author       = {{Paulsson, Marie and Dejmek, Petr}},
  issn         = {{1525-3198}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{590--600}},
  publisher    = {{American Dairy Science Association}},
  series       = {{Journal of Dairy Science}},
  title        = {{Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry}},
  url          = {{http://dx.doi.org/10.3168/jds.S0022-0302(90)78707-3}},
  doi          = {{10.3168/jds.S0022-0302(90)78707-3}},
  volume       = {{73}},
  year         = {{1990}},
}