Role of protein-protein interactions on protein aggregation and emulsion flocculation

Research output: Thesisinternal PhD, WUAcademic

Abstract

 In this thesis, the effect of molecular properties on the aggregation and flocculation behaviour is studied. The aggregation behaviour was thought to be mainly affected by the structural stability of the protein. A decreased structural stability results in unfolded proteins which are more prone to aggregation. The flocculation behaviour was shown to be affected by the adsorbed amount at saturation and the adsorption rate. These parameters have been combined in a surface coverage model, which describes the stabilization of emulsions away from the iso‑electric point (pI) to be affected by excess protein in the continuous phase. In addition, a model was proposed for the prediction of the adsorbed amount at saturation. This is influenced by the protein charge and radius and system conditions (i.e. pH and ionic strength). The adsorption rate, which is a measure for the affinity of the protein towards the adsorption to the interface, was shown to increase with increasing relative exposed hydrophobicity and a decrease of the electrostatic repulsion (i.e. decrease of ionic strength or the protein charge). Close to the pI, the applicability of protein-stabilized emulsions is limited. Hence, a steric interaction was introduced to stabilize the emulsion. It was shown that glycation of the protein with a trisaccharide was sufficient to sterically stabilize the emulsions against pH-induced flocculation.

 

LanguageEnglish
QualificationDoctor of Philosophy
Awarding Institution
  • Wageningen University
Supervisors/Advisors
  • Gruppen, Harry, Promotor
  • Wierenga, Peter, Co-promotor
Award date19 Sep 2014
Place of PublicationWageningen
Publisher
Print ISBNs9789462570054
Publication statusPublished - 2014

Fingerprint

Flocculation
Emulsions
Agglomeration
Proteins
Ionic strength
Adsorption
Trisaccharides
Hydrophobicity
Electrostatics
Stabilization

Keywords

  • methane production
  • electrochemistry
  • carbon dioxide
  • electrolysis
  • microbial fuel cells
  • sustainable energy

Cite this

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title = "Role of protein-protein interactions on protein aggregation and emulsion flocculation",
abstract = " In this thesis, the effect of molecular properties on the aggregation and flocculation behaviour is studied. The aggregation behaviour was thought to be mainly affected by the structural stability of the protein. A decreased structural stability results in unfolded proteins which are more prone to aggregation. The flocculation behaviour was shown to be affected by the adsorbed amount at saturation and the adsorption rate. These parameters have been combined in a surface coverage model, which describes the stabilization of emulsions away from the iso‑electric point (pI) to be affected by excess protein in the continuous phase. In addition, a model was proposed for the prediction of the adsorbed amount at saturation. This is influenced by the protein charge and radius and system conditions (i.e. pH and ionic strength). The adsorption rate, which is a measure for the affinity of the protein towards the adsorption to the interface, was shown to increase with increasing relative exposed hydrophobicity and a decrease of the electrostatic repulsion (i.e. decrease of ionic strength or the protein charge). Close to the pI, the applicability of protein-stabilized emulsions is limited. Hence, a steric interaction was introduced to stabilize the emulsion. It was shown that glycation of the protein with a trisaccharide was sufficient to sterically stabilize the emulsions against pH-induced flocculation.  ",
keywords = "methaanproductie, elektrochemie, kooldioxide, elektrolyse, microbi{\"e}le brandstofcellen, duurzame energie, methane production, electrochemistry, carbon dioxide, electrolysis, microbial fuel cells, sustainable energy",
author = "R.J.B.M. Delahaije",
note = "WU thesis 5848",
year = "2014",
language = "English",
isbn = "9789462570054",
publisher = "Wageningen University",
school = "Wageningen University",

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Delahaije, RJBM 2014, 'Role of protein-protein interactions on protein aggregation and emulsion flocculation', Doctor of Philosophy, Wageningen University, Wageningen.

Role of protein-protein interactions on protein aggregation and emulsion flocculation. / Delahaije, R.J.B.M.

Wageningen : Wageningen University, 2014. 158 p.

Research output: Thesisinternal PhD, WUAcademic

TY - THES

T1 - Role of protein-protein interactions on protein aggregation and emulsion flocculation

AU - Delahaije, R.J.B.M.

N1 - WU thesis 5848

PY - 2014

Y1 - 2014

N2 -  In this thesis, the effect of molecular properties on the aggregation and flocculation behaviour is studied. The aggregation behaviour was thought to be mainly affected by the structural stability of the protein. A decreased structural stability results in unfolded proteins which are more prone to aggregation. The flocculation behaviour was shown to be affected by the adsorbed amount at saturation and the adsorption rate. These parameters have been combined in a surface coverage model, which describes the stabilization of emulsions away from the iso‑electric point (pI) to be affected by excess protein in the continuous phase. In addition, a model was proposed for the prediction of the adsorbed amount at saturation. This is influenced by the protein charge and radius and system conditions (i.e. pH and ionic strength). The adsorption rate, which is a measure for the affinity of the protein towards the adsorption to the interface, was shown to increase with increasing relative exposed hydrophobicity and a decrease of the electrostatic repulsion (i.e. decrease of ionic strength or the protein charge). Close to the pI, the applicability of protein-stabilized emulsions is limited. Hence, a steric interaction was introduced to stabilize the emulsion. It was shown that glycation of the protein with a trisaccharide was sufficient to sterically stabilize the emulsions against pH-induced flocculation.  

AB -  In this thesis, the effect of molecular properties on the aggregation and flocculation behaviour is studied. The aggregation behaviour was thought to be mainly affected by the structural stability of the protein. A decreased structural stability results in unfolded proteins which are more prone to aggregation. The flocculation behaviour was shown to be affected by the adsorbed amount at saturation and the adsorption rate. These parameters have been combined in a surface coverage model, which describes the stabilization of emulsions away from the iso‑electric point (pI) to be affected by excess protein in the continuous phase. In addition, a model was proposed for the prediction of the adsorbed amount at saturation. This is influenced by the protein charge and radius and system conditions (i.e. pH and ionic strength). The adsorption rate, which is a measure for the affinity of the protein towards the adsorption to the interface, was shown to increase with increasing relative exposed hydrophobicity and a decrease of the electrostatic repulsion (i.e. decrease of ionic strength or the protein charge). Close to the pI, the applicability of protein-stabilized emulsions is limited. Hence, a steric interaction was introduced to stabilize the emulsion. It was shown that glycation of the protein with a trisaccharide was sufficient to sterically stabilize the emulsions against pH-induced flocculation.  

KW - methaanproductie

KW - elektrochemie

KW - kooldioxide

KW - elektrolyse

KW - microbiële brandstofcellen

KW - duurzame energie

KW - methane production

KW - electrochemistry

KW - carbon dioxide

KW - electrolysis

KW - microbial fuel cells

KW - sustainable energy

M3 - internal PhD, WU

SN - 9789462570054

PB - Wageningen University

CY - Wageningen

ER -