Abstract
n this work the study of adsorption immobilization of inulinase on super-crosslinked macroporous sorbents based on styrene and divinylbenzene: low-base anion exchanger A100, high-base anion exchanger A500R, strong acid cation exchanger C100H was carried out. The influence of the duration of the sorption process, the value of the concentration of hydrogen ions and the concentration of protein in solution on the amount of immobilized enzyme and the activity of the obtained heterogeneous biocatalysts is considered. It was revealed that adsorption reaches its max-imum value on average after 4 h at pH of 4.7-5.0 for the sorbents under consideration. The activity of the obtained heterogeneous biocatalysts is 64.8-83.5% of the activity of free inulinase. Although the activity of inulinase during adsorption on the polymer carriers used in the work decreases, the integral amount of the resulting product will be higher than for the native catalyst.The isotherms of inulinase adsorption on super-crosslinked polymers have been studied. The high stability of the obtained heterogeneous biocatalysts is explained by the high sorption capacity of super-crosslinkedsorbents. It was revealed that immobilized inulinase can be used during 8-11 consecutive cycles of the substrate hydrolysis reaction.Using the BET adsorption theory, the enzyme sorption isotherms were analyzed and the equilibrium sorption parameters werecalculated: the maximum amount of sorbed inulinase, the constants characterizing the sorbate-sorbent and sorbate-sorbate interaction. Among the considered carriers, the highest value of the sorption equilibrium constant (KL=4.25±0.04 l/mmol) corresponds to the inulinase-cation exchanger biocatalyst, the sorption ca-pacity of which is also the largest. The data obtained is of interest for evaluating the effectiveness of the use of sorbents as inulinase carriers in subsequent technological operations of processing of inulin-containing raw materials.
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