The impact on acrylamide formation of several additives was investigated as well as the mechanisms behind it. In a potato powder model system, sodium acid pyrophosphate, citric, acetic and L-lactic acid significantly reduced the final acrylamide content, merely due to the lowering of the pH. Free glycine, L-lysine and L-cysteine also lowered acrylamide, while keeping the pH at its original level. L-glutamine increased the formation of acrylamide. A synergistic acrylamide lowering effect was observed, adding citric acid and glycine or L-lysine to the model system. Yet, a combination of these amino acids with acetic acid appeared to induce a restricted antagonistic acrylamide lowering effect. Calcium and magnesium ions induced a supplementary acrylamide reduction in addition to a lower pH of the food matrix. No lowering effect was however observed upon NaCl addition to the model system.

Pyrazines are specific Maillard reaction compounds known to contribute to the unique aroma of many products. Most studies concerning the generation of pyrazines in the Maillard reaction have focused on amino acids, while little information is available on the impact of peptides and proteins. The present study investigated the generation of pyrazines in model systems containing whey protein, hydrolyzed whey protein, amino acids, and glucose. The impact of thermal conditions, ratio of reagents, and water activity (a(w)) on pyrazine formation was measured by headspace solid-phase microextraction with gas chromatography/mass spectrometry (HS-SPME-GC/MS. The presence of oligopeptides from hydrolyzed whey protein contributed significantly to an increased amount of pyrazines, while in contrast free amino acids generated during protein hydrolysis contributed to a lesser extent. The generation of pyrazines was enhanced at low a(w) (0.33) and high temperatures (>120 °C). This study showed that the role of peptides in the generation of pyrazines in Maillard reaction systems has been dramatically underestimated.

Hypochlorous and peracetic acids, both known disinfectants in the food industry, were compared for their oxidative capacity toward dairy proteins. Whey proteins and caseins were oxidized under well controlled conditions at pH 8 as a function of the sanitizing concentration. Different markers for protein oxidation were monitored. The results established that the protein carbonyl content was a rather unspecific marker for protein oxidation, which did not allow one to differentiate the oxidant used especially at the lower concentrations. Cysteine, tryptophan, and methionine were proven to be the most vulnerable amino acids for degradation upon hypochlorous and peracetic acid treatment, while tyrosine was only prone to degradation in the presence of hypochlorous acid. Hypochlorous acid induced oxidation gave rise to protein aggregation, while during peracetic acid induced oxidation, no high molecular weight aggregates were observed. Protein aggregation upon hypochlorous acid oxidation could primarily be linked to tryptophan and tyrosine degradation.

Food allergy represents an important food safety issue because of the potential lethal effects; the only effective treatment is the complete removal of the allergen involved from the diet. However, due to the growing complexity of food formulations and food processing, foods may be unintentionally contaminated via allergen-containing ingredients or cross-contamination. This affects not only consumers' well-being but also food producers and competent authorities involved in inspecting and auditing food companies. To address these issues, the food industry and control agencies rely on available analytical methods to quantify the amount of a particular allergic commodity in a food and thus to decide upon its safety. However, no "gold standard methods" exist for the quantitative detection of food allergens. Nowadays mostly receptor-based methods and in particular commercial kits are used in routine analysis. However, upon evaluation of their performances, commercial assays proved often to be unreliable in processed foods, attributed to the chemical changes in proteins that affect the molecular recognition with the receptor used. Unfortunately, the analytical outcome of other methods, among which are chromatographic combined with mass spectrometric techniques as well as DNA-based methods, seem to be affected in a comparable way by food processing. Several strategies can be employed to improve the quantitative analysis of allergens in foods. Nevertheless, issues related to extractability and matrix effects remain a permanent challenge. In view of the presented results, it is clear that the food industry needs to continue to make extra efforts to provide accurate labeling and to reduce the contamination with allergens to an acceptable level through the use of allergen risk management on a company level, which needs to be supported inevitably by a tailor-validated extraction and detection method.

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