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Effect of polar lipids on heat induced changes in concentrated milk systems

Marios Kasinos (2014)
abstract
During the last decades, several researchers tried to clarify and fully explain the exact mechanism of the heat-induced coagulation which occurs during heating milk at elevated temperatures. Based on literature data, this phenomenon is mainly a consequence of heat denaturation and unfolding of the globular whey protein fraction of milk, which results in the exposure of the previously buried hydrophobic and free thiol groups. As the denaturation process proceeds, several interactions start to take place leading to the formation of a product with modified organoleptic and physicochemical characteristics. The most important interactions which are believed to take place during heating milk at high temperatures are the interactions between denatured whey proteins with themselves and/or the complex formation of denatured whey proteins (or whey protein aggregates) with casein micelles. The heat-induced network between milk proteins is essentially built due to the hydrophobic bonding between the denatured whey proteins, as well as the thiol-disulfide exchange between the denatured whey proteins with themselves and/or with the κ-caseins. In order to be able to apply high temperatures and at the same time to decrease the degree of protein complexation, the application of surface active molecules (surfactants) has been proposed. Previous studies described that the effect of surfactants on the heat stability of whey protein containing emulsions is based on the protein displacement or interaction with proteins bound on the oil interface, and/or interaction with free proteins in solution.
Please use this url to cite or link to this publication:
author
promoter
UGent
organization
year
type
dissertation
publication status
published
subject
keyword
Milk proteins, Milk, Heat treatment, Phospholipids, Heat stability, Heat coagulation
pages
IV, 199 pages
publisher
Ghent University. Faculty of Bioscience Engineering
place of publication
Ghent, Belgium
defense location
Gent : Faculteit Bio-ingenieurswetenschappen (E1.015)
defense date
2014-10-17 15:00
ISBN
9789059897359
language
English
UGent publication?
yes
classification
D1
copyright statement
I have transferred the copyright for this publication to the publisher
id
5721342
handle
http://hdl.handle.net/1854/LU-5721342
date created
2014-10-13 15:34:43
date last changed
2017-10-19 22:30:09
@phdthesis{5721342,
  abstract     = {During the last decades, several researchers tried to clarify and fully explain the exact mechanism of the heat-induced coagulation which occurs during heating milk at elevated temperatures. Based on literature data, this phenomenon is mainly a consequence of heat denaturation and unfolding of the globular whey protein fraction of milk, which results in the exposure of the previously buried hydrophobic and free thiol groups. As the denaturation process proceeds, several interactions start to take place leading to the formation of a product with modified organoleptic and physicochemical characteristics. The most important interactions which are believed to take place during heating milk at high temperatures are the interactions between denatured whey proteins with themselves and/or the complex formation of denatured whey proteins (or whey protein aggregates) with casein micelles. The heat-induced network between milk proteins is essentially built due to the hydrophobic bonding between the denatured whey proteins, as well as the thiol-disulfide exchange between the denatured whey proteins with themselves and/or with the \ensuremath{\kappa}-caseins. 
In order to be able to apply high temperatures and at the same time to decrease the degree of protein complexation, the application of surface active molecules (surfactants) has been proposed. Previous studies described that the effect of surfactants on the heat stability of whey protein containing emulsions is based on the protein displacement or interaction with proteins bound on the oil interface, and/or interaction with free proteins in solution.},
  author       = {Kasinos, Marios},
  isbn         = {9789059897359},
  keyword      = {Milk proteins,Milk,Heat treatment,Phospholipids,Heat stability,Heat coagulation},
  language     = {eng},
  pages        = {IV, 199},
  publisher    = {Ghent University. Faculty of Bioscience Engineering},
  school       = {Ghent University},
  title        = {Effect of polar lipids on heat induced changes in concentrated milk systems},
  year         = {2014},
}

Chicago
Kasinos, Marios. 2014. “Effect of Polar Lipids on Heat Induced Changes in Concentrated Milk Systems”. Ghent, Belgium: Ghent University. Faculty of Bioscience Engineering.
APA
Kasinos, M. (2014). Effect of polar lipids on heat induced changes in concentrated milk systems. Ghent University. Faculty of Bioscience Engineering, Ghent, Belgium.
Vancouver
1.
Kasinos M. Effect of polar lipids on heat induced changes in concentrated milk systems. [Ghent, Belgium]: Ghent University. Faculty of Bioscience Engineering; 2014.
MLA
Kasinos, Marios. “Effect of Polar Lipids on Heat Induced Changes in Concentrated Milk Systems.” 2014 : n. pag. Print.