Barbara Kerkaert

Effects of food composition on the inactivation of foodborne microorganisms by chlorine dioxide.

Chlorine dioxide (ClO2) is a strong oxidizing agent that can be applied in solution as well as in the gaseous state. It has bactericidal, fungicidal and viricidal properties. Several food-related microorganisms, including Gram-negative and Gram-positive bacteria, yeasts, mould spores and Bacillus cereus spores were tested for their susceptibility to 0.08 mg/L gaseous ClO2 during 1 min at a relative humidity of 90%. In this screening, the resistance of the different groups of microorganisms towards gaseous ClO2 generally increased in the order Gram-negative bacteria, Gram-positive bacteria, yeasts and mould spores and Bacillus cereus spores. With this treatment, reductions of microbial numbers between 0.1 and 3.5 log cfu/cm2 could be achieved. The effects of the food components starch, fat, protein and NaCl on the antimicrobial activity of gaseous ClO2 were also evaluated. Soluble starch, corn oil, butter, whey protein isolate and NaCl were added in incremental concentrations to portions of an agar medium. Then, plates of the supplemented agars were inoculated with Leuconostoc mesenteroïdes at numbers of 4 log cfu/cm2 and subsequently treated with ClO2. Both soluble starch and NaCl did not have an effect on the antimicrobial efficiency of ClO2. However, butter, corn oil or whey protein in the agar almost eliminated the antimicrobial effect of ClO2. In corn oil-water emulsions treated with gaseous ClO2 the peroxide value increased significantly, indicating the formation of primary oxidation products. Similarly, a treatment with ClO2 increased the protein carbonyl content and induced the transformation of SH-groups to -S-S-groups in whey protein. The findings suggest that gaseous ClO2 will be a highly effective decontaminating agent for carbohydrate-rich foods, but that it would be less effective for the decontamination of high-protein and fatty foods.

Hypochlorous and Peracetic Acid Induced Oxidation of Dairy Proteins

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.

Implementation of acrylamide mitigation strategies on industrial production of French fries: challenges and pitfalls

This study evaluated various additives or process aids on the industrial production of French fries, based on their acrylamide mitigation potential and other quality parameters. The application of acetic and citric acid, calcium lactate and asparaginase was investigated on the production of frozen par-fried French fries at the beginning and end of the 2008 and 2009 potato storage season. Despite the fact that some of these treatments significantly reduced acrylamide content of the final product in preliminary laboratory experiments, their application on the industrial production of French fries did not result in additional acrylamide reductions compared to the standard product. Asparaginase was additionally tested in a production line of chilled French fries (not par-fried). Since for this product a longer enzyme-substrate contact time is allowed, a total asparagine depletion was observed for the enzyme treated fries after four days of cold storage. French fries upon final frying presented acrylamide contents below the limit of detection (12.5 μg kg⁻¹) with no effects on the sensorial properties of the final product.

The impact of photo-induced molecular changes of dairy proteins on their ACE-inhibitory peptides and activity

Among all dietary proteins, dairy proteins are the most important source of bio-active peptides which can, however, be affected by modifications upon processing and storage. Since it is still unknown to which extent the biological activity of dairy proteins is altered by chemical reactions, this study focuses on the effect of photo-induced molecular changes on the angiotensin I converting enzyme (ACE) inhibitory activity. Milk proteins were dissolved in phosphate buffer containing riboflavin and stored under light at 4°C for one month during which the molecular changes and the ACE-inhibitory activity were analysed. An increase in the total protein carbonyls and the N-formylkynurenine content was observed, besides a decrease in the free thiol, tryptophan, tyrosine and histidine content. These changes were more severe in caseins compared with whey proteins and resulted moreover in the aggregation of caseins. Due to these photo-induced molecular changes, a significant loss of the ACE-inhibitory activity was observed for casein peptides. A peptide analysis moreover illustrated that the decreased activity was not attributed to a reduced digestibility but to losses of specific ACE-inhibitory peptides. The observed molecular changes, more specifically the degradation of specific amino acids and the casein aggregation, could be assigned as the cause of the altered peptide pattern and as such of the loss in ACE-inhibitory activity.

Identification of Modified Lysozyme Peptides upon Photo-oxidation by LC-TOF-MS

Protein oxidation can have major implications on the quality and safety of foods, but the majority of methods to evaluate oxidative damage lack specificity. Therefore, this study aimed to identify specific markers for protein oxidation. A well-characterized protein, lysozyme, was modified by photo-oxidation and subsequently hydrolyzed prior to peptide analysis by LC-TOF-MS. A semiquantitative analysis of the peptides indicated that from the seven peptides containing sensitive amino acids, two peptides (HGLDNYR and WWCNDGR) were highly affected upon photo-oxidation and have the potential to serve as markers for protein oxidation. Site-specific modifications enabled the description of the degradation pathway of several lysozyme peptides but also indicated that the surrounding amino acids and the 3D structure of the protein have an impact on the induced modifications. It is therefore advisable to evaluate protein oxidation on the intact protein.