The influence of solvent concentrations and column temperatures on the separation of gliadin proteins effectiveness by RP-HPLC
2018
Gojković, Vesna | Grujić, Radoslav | Marjanović-Balaban, Ţeljka | Torbica, Aleksandra (https://orcid.org/0000-0002-9627-1598)
Gliadins are proteins from wheat flour, which are present in the daily diet of most people and animals due to their favorable amino acid composition. However, in a number of people, these proteins may have a negative effect on health. The most severe cases are described in medicine as a celiac disease. In the flour obtained by grinding grain cereals there are several dozen proteins, whose common characteristic is that they are soluble in aqueous alcohol. They are labeled as gliadins. Only some of them are responsible for the occurrence of allergic manifestations in sensitive individuals. The quality of results depends of the solvent concentrations, and the column temperatures during the chromatographic separation. Gliadin proteins have been extracted with three different isopropanol concentrations (50%, 60% and 70% v/v). Gliadin proteins separation has been performed on C3 column using the Agilent Technologies 1260 Infinity apparatus. During the proteins separation, the column has been heated at 40 °C, 45 °C and 50 °C. During the extraction of gliadin proteins with 50% (v/v) isopropanol, the highest number of proteins was observed at a column temperature of 45 °C and was 28, and the smallest at a 40 °C column temperature was 21. By extraction with 60% (v/v) isopropanol, the highest number was observed at a column temperature of 45 °C and amounted to 25, and the smallest at a column temperature of 40 °C and amounted to 23, and by extraction with 70% (v/v) isopropanol, the highest number of gliadin fractions was detected at a column temperature of 45 °C and it amounted to 27, and the smallest at a column temperature of 40 °C was 15.
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