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Introduction. The number of people with celiac disease is rapidly increasing. Gluten, is one of the most common food allergens, consists of two fractions: gliadins and glutenins. The research objective was to determine the optimal conditions for estimating gliadins by using enzyme-linked immunosorbent assay (ELISA). Study objects and methods. The experiment involved wheat flour samples (0.10; 0.20, 0.25, 0.50, and 1.0 g) suspended in different solvents (ethanol, methanol, 1-propanol, and isopropanol) of different concentrations (40, 50, 60, 70, 80, and 90% v/v). The samples were diluted with Tris buffer in ratios of 1:50, 1:100, 1:150, and 1:200. The gliadin test was performed using a Gliadin/Gluten Biotech commercial ELISA kit (Immunolab). Results and discussion. The optimal conditions for determining gliadin proteins that provided the highest gliadin concentration were: solvent – 70% v/v ethanol, extract:Tris buffer ratio – 1:50, and sample weight – 1.0 g. Conclusion. The obtained results can be of great importance to determine gliadin/gluten concentrations in food products by rapid analysis methods.

Introduction. Gliadin proteins are one of the gluten fractions. They are soluble in alcoholic solution and divided into four groups (α + β, γ, ω1.2, and ω5-gliadins). In this paper gliadins were extracted from wheat flour, and optimal conditions for their separation were determined. Study objects and methods. The separation was performed by capillary gel electrophoresis on Agilent apparatus, CE 7100 (a capillary with an inner diameter of 50 μm, a total length of 33 cm, and an effective length of 23.50 cm). In order to determine the optimal conditions, different solvent concentrations (50, 60, and 70% ethanol), capillary temperatures (20, 25, 30, 35, and 40°C), and electrode voltages (–14.5, –16.5, –17.5 and –18.5 kV) were applied. Migration time and relative concentration of each protein molecules within gliadin fractions in the electrophoregram were analysed using Agilent ChemStation Software. Results and discussion. The optimal conditions for gliadin separation were: solvent 70% (v/v) ethanol, capillary temperature of 25°C, and electrode voltage of –16.5 kV. Under these conditions, the total proteins were indetified as Xav = 23.50, including α + β gliadin fraction (Xav = 7.50 and relative concentration RC = 28.29%), γ-gliadins (Xav = 5.00, RC = 26.66%), ω1.2-gliadins (Xav = 4.33, RC = 14.93%), and ω5-gliadins (Xav = 6.67, RC = 30.98%). Conclusion. The results of the research can be of fundamental importance in the study of gluten proteins and the influence of technological procedures on their change and the possibility of reducing the allergic effect of gluten during processing.

Training of personel who are engaged in food safety management system implementation and personel who handle with food is very important for efficiency of food safety management system. Companeis very offten has a problem with assessing food safety knowledge because in standards are not defined methodlogy for this assessment. In this research we try to explore level of knowledge obout food safety amnog HACCP team members and food handlers in Bosnia and Herzegovina. A structural food safety knowledge questeionarie was developed for assessing knowledge separate for HACCP team members ad food handlers. Data were collected from 80 HACCP team members and 740 food handlers. A majoriti of HACCP team members (70,0%) has food safety training in previous three years Also, food handlers in most cases has apropriate food safety training in previous three years (80,1%). The overall test result were 83,63 % of correct answers for food handlers and 72,33% for HACCP team members. It is also sigificant that the HACCP team members has a better result in companies who are certify according one of GFSI approved certification sheme. It is recommended to companies, associations of companies, scientific institutions, consulting organisations to develop specific food safety training on higher level for HACCP team members and methodology for official assessment of food safety knowledge.

The paper analyses the effect of cooling/heating rate of chicken meat (Pectoralis major) on the crystallization temperature (Tcon, Tc, Tcend), melting temperature (Tmon, Tm, Tmend), crystallization enthalpy (ΔHc) and melting enthalpy (ΔHm). Chicken meat samples were scanned by differential scanning calorimetry (DSC) at five rates (2, 5, 10, 15, 20 °C/min), from 20 °C to -40 °C, and then from -40 °C to 20 °C.The results of the statistical analysis show that the fastest cooling rate (20 °C/min) significantly (p

peer-reviewed, The aim of this study was to test the influence of scanning rate and meat type, on the thermophysical properties of meat and content of the freezable water in frozen meat, using the differential scanning calorimetry (DSC) method. In this study three types of meat were investigated: beef (M. Longissimus dorsi), pork (M. Longissimus dorsi) and chicken meat (Pectoralis major). The cooling rate affected the onset (Tcon), peak (Tc) and end (Tcend) temperatures of crystallization process of beef meat (p

During the tests in this paper, meat processing was carried out at different temperatures between the range of 51°C to 100°C. The meat was processed by dry heat (roasting) and wet heat treatments (cooking) in water at atmospheric pressure. After heat treatment, myofibrillar proteins were extracted from solutions at constant ionic strength. Quantitative and qualitative determinations of protein´s fractions were performed by capillary electrophoresis. Myofibrillar proteins were also analized for fresh pork meat sample. Results obtained in fresh meat were compared with those recorded after roasting and cooking. In the fresh and thermally processed pork the following proteins were identified: myosin, light chain 3; myosin, light chain 2; troponin - C; troponin - I; myosin, light chain 1; tropomyosin; troponin - T; actin; desmin; α - actinin; C - protein; M - protein (Mβ); M - protein (Mα); heavy meromyosin - HMM. For both methods of thermal processing, with increasing heat treatment temperature, concentration of soluble protein in the extract decreases rapidly after 51°C. Cooking treatment had a more intense effect on the proteins change and denaturation than roasting. [Projekat Ministartsva nauke Republike Srbije: Effect of heat treatment temperature on protein structure and properties of pork meat]

Meso je veoma bitna namirnica u ishrani ljudi zbog svojih nutritivno vrijednih sastojaka. Gotovo svi proizvodi od mesa se na neki način toplotno obrađuju kako bi se postigle željene senzorne i nutritivne osobine, kao i zadovoljili kriterijumi po pitanju mikrobiološke stabilnosti i bezbijednosti proizvoda. Najčešća su dva tipa toplotne obrade u industrijskim uslovima, a to su toplotna obrada kuvanjem na atmosferskom pritisku ili vakumu i suva toplotna obrada pečenjem. Stoga ovaj rad ima za cilj dati kratak pregled najnovijih dostignuća u pogledu uticaja tehnoloških parametara tokom toplotne obrade u prvom planu visine temperature u centru uzorka i razlučitih postupaka toplotne obrade (kuvanjem i pečenjem) na promjene na proteinima, boji mesa, reološkim osobinama mesa, pH mesa, sposobnosti vezivanja vode, hemijskim osobinama i senzornim osobinama mesa., Meat is a very important food in the diet of people, due to its valuable nutritional ingredients. Almost all of the meat products are somehow heat treated to achieve the desired sensory and nutritional properties, as well as meet the criteria in terms of microbial stability and safety of the product. The most common are the two types of heat treatment in industrial conditions, such as heat treatment by cooking at atmospheric pressure or vacuum and dry heat treatment by roasting. Therefore, goal of this paper is to give a brief overview of the latest developments, regarding the influence of technological parameters during thermal processing of meat. Temperature level in the center of the sample and different thermal treatment procedures (cooking and roasting) were monitored in terms of impact on the protein’s structure changes, meat color, rheological properties of meat, meat pH, water holding capacity, chemical properties and organoleptic characteristics of meat.