Sorption of Phenylalanine from Phosphate-Containing Solutions by KU-2-4 and KU-2-8 Sulfocation Exchangers
DOI:
https://doi.org/10.17308/sorpchrom.2026.26/13699Keywords:
sorption isotherm, phenylalanine, cation exchanger, non-exchange sorption, ion exchange, sodium (di)hydrogen phosphate.Abstract
One of the modern and effective methods for isolating amino acids and proteins from biotechnological media is the use of enzymatic hydrolysis. To establish a constant pH value during hydrolysis, various buffers are used, in particular, phosphate buffers. Therefore, it is relevant to study the influence of phosphate buffer components on the sorption of amino acids. In this work, the features of phenylalanine sorption from solutions containing sodium (di)hydrogen phosphate were investigated using the strongly acidic cation exchangers KU-2-4 and KU-2-8 in salt (Na+) ionic form. The objects of the study were individual solutions of L-phenylalanine (concentration range (10.0-100.0)∙10-3 M), as well as solutions of it mixed with sodium (di)hydrogen phosphate (salt concentration 4.0∙10-3 M). The concentration of phenylalanine was determined using UV spectrophotometry at 257 nm and the concentration of phosphates were determined photometrically at 882 nm. Sorption was carried out under static conditions at a temperature of 298±2 K. It was shown that the mechanism of phenylalanine sorption depends on the composition of the solution. During sorption from individual solutions, the process proceeded according to a non-exchange absorption mechanism and is described by the Langmuir model. The addition of sodium dihydrogen phosphate led to the recharging of phenylalanine in solution with the formation of cations and bipolar ions, which leads to the implementation of two absorption mechanisms – non-exchange and ion-exchange. When using sodium hydrogen phosphate, sorption occurred via a non-exchange mechanism and was less intense, which was associated with the formation of anionic forms of phenylalanine. It was found that the maximum sorption of phenylalanine was observed in the presence of sodium dihydrogen phosphate, and the minimum was observed with the addition of sodium hydrogen phosphate.
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