Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry
(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)(Less)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.Please use this url to cite or link to this publication: https://lup.lub.lu.se/record/339ce43b-3ce4-440b-83a1-ed58db28550f- author
- Paulsson, Marie
LU
and Dejmek, Petr LU
- organization
- publishing date
- 1990
- 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}}, }