Abstracts Category : Other

Of proteins and processing: mechanisms of protein damage upon rapeseed processing and their effects on nutritional value

by Villanea Sergio Salazar

Hydrothermal processing is a common practice during the manufacture of protein-rich feed ingredients, such as rapeseed meal (RSM), and feeds. This processing step can induce physical and chemical changes to the proteins, thereby reducing the digestibility and utilization of crude protein (CP) and amino acids (AA). Whilst most literature has linked the chemical changes to the proteins with negative effects on protein digestibility, the effects of the physical changes of the protein conformation have not been considered simultaneously. Hence, the aim of this thesis was to provide further insight into the mechanisms of protein damage during ingredient/feed processing and their effects on protein hydrolysis/digestibility. In Chapter 2, the available literature on the physical changes that occur to vegetable proteins used in swine diets after processing was reviewed. Overall, hydrothermal processing increases the contents of intermolecular/intramolecular -sheets and disulfide bonds, which were negatively correlated to protein digestibility. The correlations, however, were dependent on the type of protein analysed. When the physico-chemical changes in the proteins occur during processing of the ingredients, proteins usually become less responsive to further processing treatments. Rapeseed proteins were used as model, as this oilseed is hydrothermally processed during the oil extraction process and is further processed when incorporated in animal diets. Protein damage during production of rapeseed meal There is high variability in the nutritional value of commercial RSM. The variation is mainly due to the conditions used during the desolventization/toasting step. Therefore, the aim of the experiment in Chapter 3 was to characterize the secondary structure and chemical changes that occur during toasting of RSM and their effects on in vitro protein digestibility. A cold defatted RSM was toasted for 120 min with samples obtained every 20 min. Increasing the toasting time from 0 to 120 min increased protein denaturation by 3-fold and decreased protein solubility by 4-fold, lysine content by 23% and the reactive lysine content by 37%. The proportion of intermolecular -sheets increased after the initial 20 min of toasting, but steadily decreased thereafter. The contrary was observed for the proportion of -helices. The changes in the secondary structure of proteins were not correlated to the rest of the physical and chemical changes. Therefore, changes in the secondary structure of proteins cannot be considered good indicators of damage to proteins due to hydrothermal processing. The rate of protein hydrolysis decreased by 2-fold when toasting time was increased from 0 min to 120 min. The changes in protein solubility and lysine/reactive lysine contents were positively correlated to the rate of protein hydrolysis. Changes to the physical conformation of rapeseed proteins occur at faster rates during toasting compared to chemical changes. In Chapter 4, it was hypothesized that the decrease in theAdvisors/Committee Members: University, Wouter Hendriks, Harry Gruppen, Thomas van der Poel, E.M.A.M. Bruininx.