Currently, the use of maize dried distillers grain with solubles (DDGS) as protein source in animal feed is limited by the inferior protein quality and high levels of non-starch polysaccharides (NSP). Processing technologies and enzymes that increase NSP degradability might improve digestive utilization of DDGS, enhancing its potential as a source of nutrients for animals. The effects of various combinations of processing technologies and commercial enzyme mixtures on in vitro digestion and subsequent fermentation of DDGS were tested. Wet-milling, extrusion, and mild hydrothermal acid treatment increased in vitro protein digestion but had no effect on NSP. Severe hydrothermal acid treatments, however, effectively solubilized NSP (48-78%). Addition of enzymes did not affect NSP solubilization in unprocessed or processed DDGS. Although the cell wall structure of DDGS seems to be resistant to most milder processing technologies, in vitro digestion of DDGS can be effectively increased by severe hydrothermal acid treatments.

Protein structure influences the accessibility of enzymes for digestion. The proportion of intramolecular β-sheets in the secondary structure of native proteins has been related to a decrease in protein digestibility. Changes to proteins that can be considered positive (for example, denaturation and random coil formation) or negative (for example, aggregation and Maillard reactions) for protein digestibility can occur simultaneously during processing. The final result of these changes on digestibility seems to be a counterbalance of the occurrence of each phenomenon. Occurrence of each phenomenon depends on the conditions applied, but also on the source and type of the protein that is processed. The correlation between denaturation enthalpy after processing and protein digestibility seems to be dependent on the protein source. Heat seems to be the processing parameter with the largest influence on changes in the structure of proteins. The effect of moisture is usually limited to the simultaneous application of heat, but increasing level of moisture during processing usually increases structural changes in proteins. The effect of shear on protein structure is commonly studied using extrusion, although the multifactorial essence of this technology does not allow disentanglement of the separate effects of each processing parameter (for example, heat, shear, moisture). Although most of the available literature on the processing of feed ingredients reports effects on protein digestibility, the mechanisms that explain these effects are usually lacking. Clarifying these mechanisms could aid in the prediction of the nutritional consequences of processing conditions.

BackgroundToasting 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.ResultsThe 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.ConclusionsIncreasing 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.

Increasing clinical and experimental evidence accumulated during the past few decades supports an important role for dietary advanced glycation endproducts (AGE) in the pathogenesis of many chronic non-infectious diseases, such as type 2 diabetes, CVD and others, that are reaching epidemic proportions in the Western world. Although AGE are compounds widely recognised as generated in excess in the body in diabetic patients, the potential importance of exogenous AGE, mostly of dietary origin, has been largely ignored in the general nutrition audience. In the present review we aim to describe dietary AGE, their mechanisms of formation and absorption into the body as well as their main mechanisms of action. We will present in detail current evidence of their potential role in the development of several chronic non-infectious clinical conditions, some general suggestions on how to restrict them in the diet and evidence regarding the potential benefits of lowering their consumption.

Thermal damage to proteins can reduce their nutritional value. The effects of toasting time on the kinetics of hydrolysis, the resulting molecular weight distribution of 00-rapeseed meal (RSM) and the soluble and insoluble protein fractions separated from the RSM were studied. Hydrolysis was performed with pancreatic proteases to represent in vitro protein digestibility. Increasing the toasting time of RSM linearly decreased the rate of protein hydrolysis of RSM and the insoluble protein fractions. The extent of hydrolysis was, on average, 44% higher for the insoluble compared with the soluble protein fraction. In contrast, the rate of protein hydrolysis of the soluble protein fraction was 3–9-fold higher than that of the insoluble protein fraction. The rate of hydrolysis of the insoluble protein fraction linearly decreased by more than 60% when comparing the untoasted to the 120 min toasted RSM. Increasing the toasting time elicited the formation of Maillard reaction products (furosine, N ε-carboxymethyl-lysine and N ε-carboxyethyl-lysine) and disulfide bonds in the insoluble protein fraction, which is proposed to explain the reduction in the hydrolysis rate of this fraction. Overall, longer toasting times increased the size of the peptides resulting after hydrolysis of the RSM and the insoluble protein fraction. The hydrolysis kinetics of the soluble and insoluble protein fractions and the proportion of soluble:insoluble proteins in the RSM explain the reduction in the rate of protein hydrolysis observed in the RSM with increasing toasting time.