Effect of the desolventizing/toasting process on chemical composition and protein quality of rapeseed meal

Background： During processing in a desolventizer/toaster（DT）, rapeseed meal（RSM） is heated to evaporate the hexane and to reduce the level of heat-labile anti-nutritional factors such as glucosinolates（GSL）. However, excessive heat treatment may reduce amino acid（AA） content in addition to lower AA digestibility and availability in RSM. The objective of the present study was to produce from one batch of a 00-rapeseed variety（17 μmol GSL/g dry matter（DM）, seed grade quality） five differently processed RSM under standardized and defined conditions in a pilot plant,and to determine the impact of these different treatments on protein solubility and chemical composition, in particular with regard to contents of AA including reactive Lys（rL ys） and levels of total and individual GSL.Methods： Four RSM were exposed to wet toasting conditions（WetT C） with increasing residence time in the DT of 48,64, 76, and 93 min. A blend of these four RSM was further processed, starting with saturated steam processing（〈 100 °C）and followed by exposure to dry toasting conditions（DryT C） to further reduce the GSL content in this RSM.Results： The contents of neutral detergent fiber and neutral detergent fiber bound crude protein（CP） increased linearly（P 〈 0.05）, as residence time of RSM in the DT increased from 48 to 93 min, whereas contents of total and most individual GSL and those of Lys, rL ys, Cys, and the calculated ratio of Lys：CP and r Lys：CP decreased linearly（P ≤ 0.05）.The combination of wet heating and DryT C resulted in the lowest GSL content compared to RSM produced under WetT C, but was associated with lowest protein solubility.Conclusions： It can be concluded that by increasing residence time in the DT or using alternative processing conditions such as wet heating combined with DryT C, contents of total and individual GSL in RSM can be substantially reduced.Further in vivo studies are warranted to elucidate if and to which extent the observed differences in protein quality and GSL content between RSM may affect digestibility and bioavailability of AA in monogastric animals.

Physical and chemical changes of rapeseed meal proteins during toasting and their effects on in vitro digestibility

Background： Toasting during the production of rapeseed meal（RSM） decreases ileal crude protein（CP） and amino acid（AA） digestibility. The mechanisms that determine the decrease in digestibility have not been fully elucidated. A high protein quality, low-denatured, RSM was produced and toasted up to 120 min, with samples taken every 20 min. The aim of this study was to characterize secondary structure and chemical changes of proteins and glucosinolates occurring during toasting of RSM and the effects on its in vitro CP digestibility.Results： The decrease in protein solubility and the increase of intermolecular β-sheets with increasing toasting time were indications of protein aggregation. The contents of NDF and ADIN increased with increasing toasting time.Contents of arginine, lysine and O-methylisourea reactive lysine（OMIU-RL） linearly decreased with increasing toasting time, with a larger decrease of OMIU-RL than lysine. First-order reactions calculated from the measured parameters show that glucosinolates were degraded faster than lysine, OMIU-RL and arginine and that physical changes to proteins seem to occur before chemical changes during toasting. Despite the drastic physical and chemical changes noticed on the proteins, the coefficient of in vitro CP digestibility ranged from 0.776 to 0.750 and there were no effects on the extent of protein hydrolysis after 120 min. In contrast, the rate of protein hydrolysis linearly decreased with increasing toasting time, which was largely correlated to the decrease in protein solubility, lysine and OMIU-RL observed. Rate of protein hydrolysis was more than 2-fold higher for the untoasted RSM compared to the 120 min toasted material.Conclusions： Increasing the toasting time for the production of RSM causes physical and chemical changes to the proteins that decrease the rate of protein hydrolysis. The observed decrease in the rate of protein hydrolysis could impact protein digestion and utilization.