Effect of thermally induced denaturation on molecular interaction-response relationships of whey protein isolate based films and coatings

•The degree of denaturation has a significant influence on the cross-linking density.•Mechanical properties are significantly influenced by the cross-linking density.•The cross-linking density has only a minor effect on the barrier properties.•The cross-linking density of 100% denatured films are co...

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Published inProgress in organic coatings Vol. 104; pp. 161 - 172
Main Authors Schmid, Markus, Pröls, Sandra, Kainz, Daniel M., Hammann, Felicia, Grupa, Uwe
Format Journal Article
LanguageEnglish
Published Lausanne Elsevier B.V 01.03.2017
Elsevier BV
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Online AccessGet full text
ISSN0300-9440
1873-331X
DOI10.1016/j.porgcoat.2016.11.032

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Abstract •The degree of denaturation has a significant influence on the cross-linking density.•Mechanical properties are significantly influenced by the cross-linking density.•The cross-linking density has only a minor effect on the barrier properties.•The cross-linking density of 100% denatured films are comparable with natural rubber. The functional properties of whey protein isolate (WPI) based films and coatings have been the subject of several studies. However, quantitative information on the molecular interactions is rare. The solubility studies presented here allow qualitative statements to be made about the molecular interactions in WPI-based films. The other objective of this study was to determine the cross-linking density (CLD). Swelling studies were performed on WPI-based films containing different amounts of denatured WPI. The results of the swelling studies showed that the degree of denaturation has a significant influence on the CLD, which is directly proportional to the number of disulfide bonds in the WPI-based network. As a result, the structural stability of the polymer network was improved. The swelling studies showed that there was a significant linear increase in CLD of 1.17·10−4molcm−3 on going from 50% to 100% denatured WPI-based films (0.22·10−4molcm−3→1.39·10−4molcm−3). The solubility study showed that WPI film solubility is mainly influence by non-covalent bonds up to a degree of denaturation of 75%. In general, there was a correlation between CLD and the mechanical properties of the films. The Younǵs modulus increased by 320% on going from 25% to 100% denatured WPI-based films (26.70MPa→85.30MPa). The CLD had only a minor effect on the barrier properties of the WPI-based films. Thus, this scientific paper provides new knowledge for researchers and material developers because qualitative information about the covalent intermolecular interactions in whey protein isolate based films and coatings has been obtained for the first time.
AbstractList The functional properties of whey protein isolate (WPI) based films and coatings have been the subject of several studies. However, quantitative information on the molecular interactions is rare. The solubility studies presented here allow qualitative statements to be made about the molecular interactions in WPI-based films. The other objective of this study was to determine the cross-linking density (CLD). Swelling studies were performed on WPI-based films containing different amounts of denatured WPI. The results of the swelling studies showed that the degree of denaturation has a significant influence on the CLD, which is directly proportional to the number of disulfide bonds in the WPI-based network. As a result, the structural stability of the polymer network was improved. The swelling studies showed that there was a significant linear increase in CLD of 1.17.10-4 mol cm-3 on going from 50% to 100% denatured WPI-based films (0.22.10-4 mol cm-3 → 1.39.10-4 mol cm-3). The solubility study showed that WPI film solubility is mainly influence by non-covalent bonds up to a degree of denaturation of 75%. In general, there was a correlation between CLD and the mechanical properties of the films. The Youngis modulus increased by 320% on going from 25% to 100% denatured WPI-based films (26.70 MPa → 85.30 MPa). The CLD had only a minor effect on the barrier properties of the WPI-based films. Thus, this scientific paper provides new knowledge for researchers and material developers because qualitative information about the covalent intermolecular interactions in whey protein isolate based films and coatings has been obtained for the first time.
•The degree of denaturation has a significant influence on the cross-linking density.•Mechanical properties are significantly influenced by the cross-linking density.•The cross-linking density has only a minor effect on the barrier properties.•The cross-linking density of 100% denatured films are comparable with natural rubber. The functional properties of whey protein isolate (WPI) based films and coatings have been the subject of several studies. However, quantitative information on the molecular interactions is rare. The solubility studies presented here allow qualitative statements to be made about the molecular interactions in WPI-based films. The other objective of this study was to determine the cross-linking density (CLD). Swelling studies were performed on WPI-based films containing different amounts of denatured WPI. The results of the swelling studies showed that the degree of denaturation has a significant influence on the CLD, which is directly proportional to the number of disulfide bonds in the WPI-based network. As a result, the structural stability of the polymer network was improved. The swelling studies showed that there was a significant linear increase in CLD of 1.17·10−4molcm−3 on going from 50% to 100% denatured WPI-based films (0.22·10−4molcm−3→1.39·10−4molcm−3). The solubility study showed that WPI film solubility is mainly influence by non-covalent bonds up to a degree of denaturation of 75%. In general, there was a correlation between CLD and the mechanical properties of the films. The Younǵs modulus increased by 320% on going from 25% to 100% denatured WPI-based films (26.70MPa→85.30MPa). The CLD had only a minor effect on the barrier properties of the WPI-based films. Thus, this scientific paper provides new knowledge for researchers and material developers because qualitative information about the covalent intermolecular interactions in whey protein isolate based films and coatings has been obtained for the first time.
Author Pröls, Sandra
Schmid, Markus
Grupa, Uwe
Kainz, Daniel M.
Hammann, Felicia
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Keywords Intramolecular and intermolecular interactions
Cross-linking density
Degree of denaturation
Solubility and swelling studies
Molecular interaction-property relationships
Whey protein isolate
Language English
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Snippet •The degree of denaturation has a significant influence on the cross-linking density.•Mechanical properties are significantly influenced by the cross-linking...
The functional properties of whey protein isolate (WPI) based films and coatings have been the subject of several studies. However, quantitative information on...
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SubjectTerms Chemical bonds
Coatings
Covalent bonds
Cross-linking density
Crosslinking
Degree of denaturation
Denaturation
Density
Intramolecular and intermolecular interactions
Knowledge
Mechanical properties
Molecular interaction-property relationships
Molecular interactions
Protective coatings
Solubility
Solubility and swelling studies
Structural stability
Swelling
Whey
Whey protein isolate
Title Effect of thermally induced denaturation on molecular interaction-response relationships of whey protein isolate based films and coatings
URI https://dx.doi.org/10.1016/j.porgcoat.2016.11.032
https://www.proquest.com/docview/1946417891
Volume 104
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