The effect of electrostatic interactions on the critical percolation concentration (cp) of fibrillar -lactoglobulin gels at pH 2 was investigated using rheological measurements, transmission electron microscopy (TEM), and performing conversion experiments. A decreasing cp with increasing ionic strength was found. The fraction of nonaggregated -lactoglobulin was independent of ionic strength in the regime of 0.01-0.08 M. TEM experiments showed long fibrils (2-7 m) for ionic strengths between 0.01 and 0.08 M. Since both the conversion of monomers and the contour length of the fibrils were independent of ionic strength (0.01-0.08M), the linear increase of cp with the Debye length can be attributed purely to an increase of electrostatic repulsi...
The interaction of proteins (ß-lactoglobulin, Bovine Serum Albumin (BSA), gelatins and whey protein ...
There are a lot of works in literature about the size particle of ?-lactoglobulin (?-lg) at differen...
The objective of this study was to obtain -lactoglobulin (-lg) gels at very low protein concentratio...
The effect of electrostatic interactions on the critical percolation concentration (cp) of fibrillar...
We investigated the mesostructure of three different food proteins (ß-lactoglobulin (ß-lg), bovine s...
In order to improve the stability of β-lactoglobulin fibrils formed in acidic conditions to increase...
AbstractThe effects of electrostatic interactions and obstruction by the microstructure on probe dif...
The effects of electrostatic interactions and obstruction by the microstructure on probe diffusion w...
The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements...
We investigate the effect of ionic strength on the kinetics of heat-induced fibrilar aggregation of ...
Protein-protein interactions are essential for the understanding of biological processes. Specific p...
Properties of Fibrillar Protein Assemblies and their Percolating Networks. PhD thesis, Wageningen Un...
Abstract In this paper, we have investigated the mesoscopic structure and rheological properties of ...
pH-Induced cold gelation of whey proteins is a two-step process. After protein aggregates have been ...
Factors of ion specificity and ionic strength (I~0-100) were studied in the electrostatic complex fo...
The interaction of proteins (ß-lactoglobulin, Bovine Serum Albumin (BSA), gelatins and whey protein ...
There are a lot of works in literature about the size particle of ?-lactoglobulin (?-lg) at differen...
The objective of this study was to obtain -lactoglobulin (-lg) gels at very low protein concentratio...
The effect of electrostatic interactions on the critical percolation concentration (cp) of fibrillar...
We investigated the mesostructure of three different food proteins (ß-lactoglobulin (ß-lg), bovine s...
In order to improve the stability of β-lactoglobulin fibrils formed in acidic conditions to increase...
AbstractThe effects of electrostatic interactions and obstruction by the microstructure on probe dif...
The effects of electrostatic interactions and obstruction by the microstructure on probe diffusion w...
The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements...
We investigate the effect of ionic strength on the kinetics of heat-induced fibrilar aggregation of ...
Protein-protein interactions are essential for the understanding of biological processes. Specific p...
Properties of Fibrillar Protein Assemblies and their Percolating Networks. PhD thesis, Wageningen Un...
Abstract In this paper, we have investigated the mesoscopic structure and rheological properties of ...
pH-Induced cold gelation of whey proteins is a two-step process. After protein aggregates have been ...
Factors of ion specificity and ionic strength (I~0-100) were studied in the electrostatic complex fo...
The interaction of proteins (ß-lactoglobulin, Bovine Serum Albumin (BSA), gelatins and whey protein ...
There are a lot of works in literature about the size particle of ?-lactoglobulin (?-lg) at differen...
The objective of this study was to obtain -lactoglobulin (-lg) gels at very low protein concentratio...