Studies of the Processes of the Trypsin Interactions with Ion Exchange Fibers and Chitosan

Autor: V. G. Artyukhov, A. N. Lukin, Svetlana Pankova, Y. M. Vyshkvorkina, F. A. Sakibaev, M. G. Holyavka
Rok vydání: 2021
Předmět:
Zdroj: Russian Journal of Bioorganic Chemistry. 47:765-776
ISSN: 1608-330X
1068-1620
Popis: A localization of charged and hydrophobic amino acid residues in the trypsin molecule was studied, and a percentage of the amino acids of different types on a surface of the enzyme globule was determined. The charged and hydrophobic amino acid residues were shown to be irregularly distributed on the protein surface and to form local clusters. The VION KN-1 and VION AN-1 fibers and chitosan were found to be promising carriers for the trypsin immobilization, because an adsorption on these fibers provided the preservation of 54, 58 and 65% of the catalytic activity of the native enzyme in solution, respectively (measured according to the hydrolysis rate of the bovine serum albumin). The IR spectra of the native (free) enzyme and the enzyme immobilized on the polymeric supports were analyzed. Electrostatic interactions and hydrogen bonds were shown to be dominant during the trypsin adsorption on the VION fibers. Carboxyl groups of the VION KN-1 interacted with positively charged regions of the molecule which contained His, Lys, and Arg. A large number of amino groups of the VION AN-1 and chitosan created an excessive positive charge which, possibly, provided a binding to the negatively charged Asp and Glu. However, hydrophobic interactions in which Gly, Ala, Tyr, Val, Phe, Pro, and Leu were involved became the most important for the trypsin adsorption on chitosan.
Databáze: OpenAIRE
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