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1 Effect of protein charge on the generation of aggregation-prone conformers
article 2007    
Author: Broersen, K. · Weijers, M. · Groot, J.de · Hamer, R.J. · Jongh, H.H.J.de
Keywords: Nutrition · Food technology · Chemical modification · Conformations · Denaturation · Electrostatics · Methylation · Proteins · Temperature · Aggregation kinetics · Conformers · Electrostatic repulsive forces · Ovalbumin · Biomolecules · ovalbumin · article · conformational transition · controlled study · denaturation · electricity · heating · methylation · nonhuman · physical chemistry · priority journal · protein aggregation · protein engineering · surface charge · Animals · Electrostatics · Heat · Kinetics · Ovalbumin · Protein Denaturation · Protein Folding · Urea
[Abstract]

2 Structure and rheological properties of acid-induced egg white protein gels
article 2006    
Author: Weijers, M. · Velde, F. van de · Stijnman, A. · Pijpekamp, A. van de · Visschers, R.W.
Keywords: Nutrition · Food technology · Acid-induced gelation · Aggregation · Hen egg white proteins · Ovalbumin · Ovotransferrin · Purification · Turbidity · Whey protein isolate
[Abstract]

3 Net charge affects morphology and visual properties of ovalbumin aggregates
article 2008    
Author: Weijers, M. · Broersen, K. · Barneveld, P.A. · Cohen Stuart, M.A. · Hamer, R.J. · Jongh, H.H.J.de · Visschers, R.W.
Keywords: Nutrition · Food technology · Agglomeration · Chemical engineering · Chromatographic analysis · Electrophoresis · Morphology · Optical properties · Turbidity · Aggregate morphologies · Degree of branching · Net charges · Ovalbumin · Transmission electrons · Turbidity measurements · Visual appearances · Visual properties · Aggregates · ovalbumin · article · chemical modification · controlled study · disulfide bond · gel permeation chromatography · heating · incubation time · morphology · particle size · pH · physical chemistry · polyacrylamide gel electrophoresis · priority journal · protein aggregation · protein structure · rigidity · transmission electron microscopy · turbidity · Animals · Electrophoresis, Polyacrylamide Gel · Microscopy, Electron · Nephelometry and Turbidimetry · Ovalbumin · Pliability · Precipitation · Protein Conformation · Solubility · Static Electricity
[Abstract]

4 Acid-Induced Cold Gelation of Globular Proteins: Effects of Protein Aggregate Characteristics and Disulfide Bonding on Rheological Properties
article 2004    
Author: Alting, A.C. · Weijers, M. · Hoog, E.H.A. de · Pijpekamp, A.M. van de · Cohen Stuart, M.A. · Hamer, R.J. · Kruif, C.G. de · Visschers, R.W.
Keywords: Nutrition · Food technology · Aggregation · Cold gelation · Fibril formation · Ordered structures · Ovalbumin · Thiol-disulfide exchange reaction · Whey protein isolate · acid · cross linking reagent · Cross Linking Reagents · disulfide · globular protein · milk protein · monomer · ovalbumin · thiol derivative · thiol group · whey protein · article · chemistry · cold · covalent bond · disulfide bond · electron microscopy · fiber · flow kinetics · gel · gelation · hardness · heat treatment · pH · protein aggregation · protein isolation · randomization · whey · Cold · Cross-Linking Reagents · Disulfides · Gels · Hydrogen-Ion Concentration · Microscopy, Electron · Milk Proteins · Ovalbumin · Rheology · Sulfhydryl Compounds
[Abstract]

Search results also available in MS Excel format.

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