Food Chemistry

Food proteins

Our aim is to gain knowledge of the effect of processing on the biochemical and physicochemical properties of proteins in raw materials, ingredients and foods, in relation to their functional and nutritional properties Since proteins vary widely in their structure, their functional properties will diverge accordingly. Additional factors of influence for the functionality of proteins are isolation procedure, (physico-)chemical or enzymatic modification, and the composition and processing route of the food in which they are applied. Knowledge of structure-function relationships of proteins in foods, and the interaction between proteins and other food constituents form the basis for the development of modern processes, of new ingredients and of higher quality products.

Description of theme 

In the group there are four major research lines.

1) Novel and current plant proteins (including microalgae): Focussed at isolation methods and issues and characterization of the obtained concentrates/isolates.

2) Enzymatic hydrolysis of proteins: To describe the protein hydrolysis a method has been developed focussing on the identification and quantification of all peptides in hydrolysates taken during hydrolysis. This allowed further development of concepts to characterize this process and relevant molecular properties of both protease (selectivity) and substrate.

3) Maillard reactions: In order to understand the effects of Maillard reactions on ingredient functionality we need adequate methods to quantify the extent of modification. For this different methods are applied, improved and combined.

4) Foam- and emulsifying properties of proteins: We develop methods and concepts to describe the these properties in terms of their molecular properties.

Analytical methods used therefore range from those to determine protein conformation (CD), LC-MS, light-scattering and multiple chromatographic or electrophoretic techniques. Asymmetric flow-field flow fractionation coupled with a multi-angle light scattering detector is used for the characterisation of protein aggregates. Furthermore we have equipment to determine interfacial, foaming and emulsifying properties of proteins. This is supplemented with studies of thin liquid films studied under reflected light microscopy. To study in vitro hydrolysis we have several pH stat units. The study of proteins from several angles provides a complete overview.

Research Projects