Protein mixtures: interactions and gelation

C. Ersch

Research output: Thesisinternal PhD, WU

Abstract

Gelation is a ubiquitous process in the preparation of foods. As most foods are multi constituent mixtures, understanding gelation in mixtures is an important goal in food science. Here we presented a systematic investigation on the influence of molecular interactions on the gelation in protein mixtures. Gelatin gels with added globular protein and globular protein gels with added gelatin were analyzed for their gel microstructure and rheological properties. Mixed gels with altered microstructure (compared to single gels) also differed in modulus from single gels. Mixed gels with microstructures similar to single gels were rheologically similar to single gels. Alterations in microstructure were attributed to segregative phase separation between proteins which occurred during gelation. Gelation was treated as a growth process from macromolecule to space spanning network. At conditions where electrostatic interactions were screened the occurrence of phase separation was attributed to the molecular size ratio between gelling and non-gelling proteins before gelation and changes of this size ratio during gelation. Here only mixtures that during gelation passed a region of high compatibility (similar molecular sizes) before entering a region of decreasing solubility phase separated. For applications this implies that whenever the gelling molecule is larger than the non-gelling molecule phase separation during gelation is unlikely while reversely, if the gelling molecules is smaller than the non-gelling molecule phase separation during gelation typically does occur

Original languageEnglish
QualificationDoctor of Philosophy
Awarding Institution
  • Wageningen University
Supervisors/Advisors
  • van der Linden, Erik, Promotor
  • Martin, A.H., Co-promotor
  • Venema, Paul, Co-promotor
Award date27 Aug 2015
Place of PublicationWageningen
Publisher
Print ISBNs9789462574212
Publication statusPublished - 2015

Fingerprint

Gelation
Gels
Proteins
Phase separation
Microstructure
Molecules
Gelatin
Molecular interactions
Coulomb interactions
Macromolecules
Solubility

Keywords

  • protein
  • whey protein
  • soya protein
  • gelation
  • gelatin
  • gels
  • rheology
  • structure
  • molecular interactions

Cite this

Ersch, C. (2015). Protein mixtures: interactions and gelation. Wageningen: Wageningen University.
Ersch, C.. / Protein mixtures: interactions and gelation. Wageningen : Wageningen University, 2015. 199 p.
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abstract = "Gelation is a ubiquitous process in the preparation of foods. As most foods are multi constituent mixtures, understanding gelation in mixtures is an important goal in food science. Here we presented a systematic investigation on the influence of molecular interactions on the gelation in protein mixtures. Gelatin gels with added globular protein and globular protein gels with added gelatin were analyzed for their gel microstructure and rheological properties. Mixed gels with altered microstructure (compared to single gels) also differed in modulus from single gels. Mixed gels with microstructures similar to single gels were rheologically similar to single gels. Alterations in microstructure were attributed to segregative phase separation between proteins which occurred during gelation. Gelation was treated as a growth process from macromolecule to space spanning network. At conditions where electrostatic interactions were screened the occurrence of phase separation was attributed to the molecular size ratio between gelling and non-gelling proteins before gelation and changes of this size ratio during gelation. Here only mixtures that during gelation passed a region of high compatibility (similar molecular sizes) before entering a region of decreasing solubility phase separated. For applications this implies that whenever the gelling molecule is larger than the non-gelling molecule phase separation during gelation is unlikely while reversely, if the gelling molecules is smaller than the non-gelling molecule phase separation during gelation typically does occur",
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Ersch, C 2015, 'Protein mixtures: interactions and gelation', Doctor of Philosophy, Wageningen University, Wageningen.

Protein mixtures: interactions and gelation. / Ersch, C.

Wageningen : Wageningen University, 2015. 199 p.

Research output: Thesisinternal PhD, WU

TY - THES

T1 - Protein mixtures: interactions and gelation

AU - Ersch, C.

N1 - WU thesis no. 6097

PY - 2015

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N2 - Gelation is a ubiquitous process in the preparation of foods. As most foods are multi constituent mixtures, understanding gelation in mixtures is an important goal in food science. Here we presented a systematic investigation on the influence of molecular interactions on the gelation in protein mixtures. Gelatin gels with added globular protein and globular protein gels with added gelatin were analyzed for their gel microstructure and rheological properties. Mixed gels with altered microstructure (compared to single gels) also differed in modulus from single gels. Mixed gels with microstructures similar to single gels were rheologically similar to single gels. Alterations in microstructure were attributed to segregative phase separation between proteins which occurred during gelation. Gelation was treated as a growth process from macromolecule to space spanning network. At conditions where electrostatic interactions were screened the occurrence of phase separation was attributed to the molecular size ratio between gelling and non-gelling proteins before gelation and changes of this size ratio during gelation. Here only mixtures that during gelation passed a region of high compatibility (similar molecular sizes) before entering a region of decreasing solubility phase separated. For applications this implies that whenever the gelling molecule is larger than the non-gelling molecule phase separation during gelation is unlikely while reversely, if the gelling molecules is smaller than the non-gelling molecule phase separation during gelation typically does occur

AB - Gelation is a ubiquitous process in the preparation of foods. As most foods are multi constituent mixtures, understanding gelation in mixtures is an important goal in food science. Here we presented a systematic investigation on the influence of molecular interactions on the gelation in protein mixtures. Gelatin gels with added globular protein and globular protein gels with added gelatin were analyzed for their gel microstructure and rheological properties. Mixed gels with altered microstructure (compared to single gels) also differed in modulus from single gels. Mixed gels with microstructures similar to single gels were rheologically similar to single gels. Alterations in microstructure were attributed to segregative phase separation between proteins which occurred during gelation. Gelation was treated as a growth process from macromolecule to space spanning network. At conditions where electrostatic interactions were screened the occurrence of phase separation was attributed to the molecular size ratio between gelling and non-gelling proteins before gelation and changes of this size ratio during gelation. Here only mixtures that during gelation passed a region of high compatibility (similar molecular sizes) before entering a region of decreasing solubility phase separated. For applications this implies that whenever the gelling molecule is larger than the non-gelling molecule phase separation during gelation is unlikely while reversely, if the gelling molecules is smaller than the non-gelling molecule phase separation during gelation typically does occur

KW - eiwit

KW - wei-eiwit

KW - sojaeiwit

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KW - gelatine

KW - gels

KW - reologie

KW - structuur

KW - moleculaire interacties

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KW - whey protein

KW - soya protein

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SN - 9789462574212

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Ersch C. Protein mixtures: interactions and gelation. Wageningen: Wageningen University, 2015. 199 p.