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Different types of columns with specific structural properties were used for the separation of mixtures of ionic liquid cations. Two of them were home-made packings and the other two were commercial stationary phases. One of the home-made packings contained cholesterol ligands bonded chemically to silica (SG-CHOL) whereas the other one was a mixed stationary phase (SG-MIX) with cyanopropyl, aminopropyl, phenyl, octyl, and octadecyl ligands. RP-18e Innovation ChromolithTM Performance and Macrosphere 300 C4 packings were also used. A comparison of the separation possibilities offered by these columns for the substances in question revealed significant differences in performance. Packings containing surface-bonded functional groups that are able to undergo protonation are not suitable for separation of such compounds under the given analysis conditions (pH = 4). The best results were obtained for two alkyl stationary phases: butyl and octadecyl. Cluster analysis has also been performed for comparison of the ionic liquid cation properties.

Analysis of the modified nucleosides is particularly important in the medical area because of a possibility of cancerogenic processes studies. The aim of this work was to study the selectivity tuning of modified nucleosides through the investigations of interactions analyte (modified nucleoside) <==> stationary phase <==> mobile phase. A series of homemade stationary phases with different surface properties has been utilized. All of them contain various interaction sites such as: cholesterol (SG-CHOL); n-acylamide (SG-CHOL, SG-AP); aminopropyl (SG-CHOL, SG-AP, SG-NH2, SG-MIX); cyanopropyl, phenyl, octyl (SG-MIX), octadecyl (SG-MIX, SG-C18) and silanols localized on the silica gel surface of all packings. The attempt to predict the main interactions responsible for the retention between nucleosides and stationary phase ligands was done on the basis of the elemental analysis, and proportional part of an individual ligand bonded to silica surface results. In order to study the influence of different packing types on the analyzed nucleosides retention, the relationship between pH of the mobile phase buffer and the selectivity of a stationary phase was investigated.

The impact of meat additives on the concentration of biogenic amines and the quality of meat was studied. Fresh white and red meat samples were fortified with the following food additives: citric and lactic acids, disodium diphosphate, sodium nitrite, sodium metabisulphite, potassium sorbate, sodium chloride, ascorbic acid, α-tocopherol, propyl 3,4,5-trihydroxybenzoate (propyl gallate) and butylated hydroxyanisole. The content of spermine, spermidine, putrescine, cadaverine, histamine, tyramine, tryptamine and 2-phenylethylamine was determined by capillary isotachophoretic methods in meat samples (fresh and fortified) during four days of storage at 4°C. The results were applied to estimate the impact of the tested additives on the formation of biogenic amines in white and red meat. For all tested meats, sodium nitrite, sodium chloride and disodium diphosphate showed the best inhibition. However, cadaverine and putrescine were characterised by the biggest changes in concentration during the storage time of all the additives. Based on the presented data for the content of biogenic amines in meat samples analysed as a function of storage time and additives, we suggest that cadaverine and putrescine have a significant impact on meat quality.

In this study, dark chocolates (DCh) containing zinc lactate (ZnL) were enriched with extracts from elderberries (EFrE), elderflowers (EFlE), and chokeberries (ChFrE) to improve their functional properties. Both dried plant extracts and chocolates were analyzed for antioxidant capacity (AC) using four different analytical methods: 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), cupric ion-reducing antioxidant capacity (CUPRAC), and ferric-reducing antioxidant power (FRAP), while total phenolic content (TPC) was determined by Folin–Ciocalteu (F–C) assay. An increase in antioxidant properties of fortified chocolates was found, and the bioaccessibility of their antioxidants was evaluated. The highest AC and TPC were found in ChFrE and chocolate with chokeberries (DCh + ChFrE) before and after simulated in vitro digestion. Bioaccessibility studies indicated that during the simulated digestion the AC of all chocolates reduced significantly, whereas insignificant differences in TPC results were observed between chemical and physiological extracts. Moreover, the influence of plant extracts on physicochemical parameters such as moisture content (MC), fat content (FC), and viscosity of chocolates was estimated. Furthermore, scanning electron microscopy with dispersive energy spectroscopy (SEM-EDS) was used to analyze surface properties and differences in the chemical composition of chocolates without and with additives.

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Tryptophan is essential amino acid and precursor for many neurotramsmiters that must be obtained from dietary proteins. However, its free form is easily absorbed and could increase the availability of this amino acid to the brain. Because of free tryptophan interaction with human health simple, eco-friendliness and low-cost method of determination are still needed. In this study, new and simple procedure for free tryptophan determination using capillary isotachophoresis is discussed. The method validation pointed good linearity, satisfactory selectivity, accuracy (recoveries varied from 98.4 to 100.1%), intra-and inter-day precision (coefficent of variation was < 5% for each standard solution and < 6% for real samples) and no matrix effect. The proposed procedure was successfully applied to analyse free tryptophan in beer samples and found contents varied from not detected to 40.74 ± 0.27 mg L −1. The obtained results were compared with chromatographic determination after derivatization with 2-chloro-1,3-dinitro-5-(trifluoromethyl)benzene and pointed better selectivity and accuracy of isotachophoretic procedure with similar precision. Due to the simplicity and flexibility, the proposed procedure is suitable for tryptophan analysis in complex matrices.