Add to ORKGFood-grade biomaterials, like -lactoglobulin, bovine serum albumin, and ovalbumin, can assemble into fibrils. Using the irreversible fibril formation for -lactoglobulin, gels can be formed even at protein concentrations of 0.07%. These fibrillar mesostructures form new structuring materials for food and pharmaceutical applications
ABSTRACT Protein aggregation is a problem with a multitude of consequences, ranging from affecting p...
The objective of this doctoral thesis was to investigate the relationship between the architecture o...
Bovine β-lactoglobulin (β-Lg) self-assembles into long amyloid-like fibrils when heated at 80 °C, pH...
Biology provides us with a unique set of self-assembled fibrillar networks in the form of amyloid fi...
We investigated the mesostructure of three different food proteins (ß-lactoglobulin (ß-lg), bovine s...
BackgroundNanofibrillation of proteins by heating at extremely acidic condition for long durations (...
Properties of Fibrillar Protein Assemblies and their Percolating Networks. PhD thesis, Wageningen Un...
Protein fibrils are threadlike aggregates that are about one molecule thick and more than thousand ...
To control and enhance protein functionality is a major challenge for food scientists. In this conte...
Aqueous systems containing sodium taurodeoxycholate and, eventually, soybean lecithin were investiga...
The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements...
The development of new functional ingredients is important for future food products. This PhD resear...
Fibril formation in mixtures of whey proteins upon heating at pH 2 was investigated. Fibrils were fo...
This paper describes a low temperature, enzymatic route to induce fibrillar structures in a protein ...
Nanofibrillar forms of proteins were initially recognized in the context of pathology, but more rece...
ABSTRACT Protein aggregation is a problem with a multitude of consequences, ranging from affecting p...
The objective of this doctoral thesis was to investigate the relationship between the architecture o...
Bovine β-lactoglobulin (β-Lg) self-assembles into long amyloid-like fibrils when heated at 80 °C, pH...
Biology provides us with a unique set of self-assembled fibrillar networks in the form of amyloid fi...
We investigated the mesostructure of three different food proteins (ß-lactoglobulin (ß-lg), bovine s...
BackgroundNanofibrillation of proteins by heating at extremely acidic condition for long durations (...
Properties of Fibrillar Protein Assemblies and their Percolating Networks. PhD thesis, Wageningen Un...
Protein fibrils are threadlike aggregates that are about one molecule thick and more than thousand ...
To control and enhance protein functionality is a major challenge for food scientists. In this conte...
Aqueous systems containing sodium taurodeoxycholate and, eventually, soybean lecithin were investiga...
The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements...
The development of new functional ingredients is important for future food products. This PhD resear...
Fibril formation in mixtures of whey proteins upon heating at pH 2 was investigated. Fibrils were fo...
This paper describes a low temperature, enzymatic route to induce fibrillar structures in a protein ...
Nanofibrillar forms of proteins were initially recognized in the context of pathology, but more rece...
ABSTRACT Protein aggregation is a problem with a multitude of consequences, ranging from affecting p...
The objective of this doctoral thesis was to investigate the relationship between the architecture o...
Bovine β-lactoglobulin (β-Lg) self-assembles into long amyloid-like fibrils when heated at 80 °C, pH...